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Rosetta Informational Moderator: Mod.Zilla
We got some good news today. A manuscript that many of you contributed to through Rosetta@home was just accepted for publication in Science magazine, perhaps the most widely read scientific journal. The paper shows that accurate structures can be calculated using Rosetta for proteins up to 200 amino acids long if even a small amount of experimental data (from NMR experiments) is available to guide the search. This is an exciting advance because it could make it very much faster and easier to experimentally determine protein structures. Thanks everybody for your contributions to this work, and to our ongoing research efforts!
Sarel has collected many very promising potential flu virus inhibitors from your rosetta@home calculations over the last ten days, and will be selecting a number of them for experimental testing--see his postings in the "design of protein-protein interactions" thread.
We are entering a very busy and science packed time for Rosetta@home. As described in the "design of protein-protein interfaces" thread, we are now designing proteins to bind to and block several different targets, including the flu virus. At the same time, we are gearing up for CASP9 which will start in May by testing out both our new structure prediction methodology and the improved energy function which underlies it. The new methodology is quite CPU intensive, and we are hoping for as much user participating as possible once CASP starts; whatever you can spare now as well would be great so we can go the last 9 yards on structure prediction methods development before CASP and at the same time proceed as rapidly as possible on the protein-protein interaction designs. thanks! David
This survey request is from David Anderson, the creator of BOINC, and Oded Nov from NYU
Dear Rosetta@home volunteer:
We are conducting a survey of Rosetta@home volunteers in order to
better understand why people participate in volunteer computing and
contribute computer resources.
We would be extremely grateful if you could help us by filling out a
questionnaire. If you are not interested, ignore the rest of this
The survey is at http://boinc.berkeley.edu/survey/ It should take no
more than 10-15 minutes. Your responses will be used for research
purposes and to improve BOINC.
We will be happy to share our findings with you, and they will be made
available once we complete the data collection and analysis.
With many thanks -
Dr. David P. Anderson
Director, BOINC
University of California, Berkeley
email: davea at ssl.berkeley.edu
Prof. Oded Nov
Polytechnic Institute of New York University
email: onov at poly.edu
Our paper on solving structures of proteins of up to 200 amino acids using very limited experimental data is in the Feb 19 issue of Science magazine (pg 1014) which is on some news stands now. this wouldn't have been possible without Rosetta@home--thanks again everybody!
While the results are still preliminary, it appears that Rosetta@home has produced an extremely exciting result! As I described a few posts ago, many of you through rosetta@home contributed to the design of proteins predicted to bind very tightly to the influenza flu virus. We have now completed the first round of testing of the designed proteins, and one of them in the experiments conducted thus far clearly binds very tightly to the virus. Our data also indicate that the binding is at a site critical to the virus invasion of our cells, and so the protein may be able to neutralize the virus. I will keep you posted over the next couple of months as the picture becomes clearer--but for now--thank you all for making this possible!!
I was asked on the discussion thread about the timescale for learning more about the influenza binding protein I described in my previous post. I'm reposting my answer here:
We are doing a series of tests and control experiments in my lab in the next 2-3 weeks to rule out various possible artifacts. If, as we expect, the design passes with flying colors, we will send it to Scripps research institute where the ability of the design to neutralize the virus in cell based tests and the extent to which the design neutralizes different strains of virus will be measured. I would expect we would know the results of this in several months. We will also work to solve the crystal structure of the design bound to the virus to confirm the design binding mode. This hopefully will not take more than a few months as well.
I will keep all of you posted here about the results from these experiments. I am very optimistic, but one should be cautious about getting to excited too early about results like these--there are very many places where things can go wrong just with the biochemistry, and after this there are very many steps to actually make a protein into a drug--this is why there are so few new drugs for curing diseases being discovered.
For those of you who would like to try your hand at improving designed binders to the influenza virus, we are now posting virus inhibitor design challenges on foldit.
Experiments this past week have made us even more confident that the designed influenza binder is working as in the design model. we used "directed evolution" methods to identify amino acid changes that make the rosetta@home designed protein bind even more tightly to the virus. we found mutations at two positions: first, at an alanine residue in the design, the evolution process found a valine, and inspection of the design model showed some extra space around the alanine that would be filled by the slightly larger valine. the second amino acid change involved a charged aspartate residue in the design that in retrospect was too close to the virus protein--it was changed to a non charged residue which is less energetically costly to bury upon binding.
we are now combining these two substitutions, and expect that the combination should bind still more tightly to the virus than any protein we have tested so far. we should know later this week--I'll keep you posted!
We got some good news today in an announcement by Vice President Biden:
We were funded to work with three other research groups to develop a completely new pathway for using solar energy to transform CO2 into the large molecules that the world has grown to depend on (fuels, etc)--this if successful could greatly reduce dependence on fossil fuels and contribute to removing CO2 from the atmosphere.
While the large majority of rosetta@home calculations will remain focused on biomedical problems, expect to see from time to time work units relating to design of enzymes for CO2 capture and conversion.
We got some more good news today: a manuscript we submitted to Science magazine on rosetta based de novo design of a new enzyme which catalyzes the formation of two carbon-carbon bonds between two small molecules was accepted for publication. The work described in the manuscript is a real step forward in designing enzyme catalysts for reactions not catalyzed by naturally occurring enzymes, and could provide new routes to drug molecules which can be hard to synthesize using traditional methods.
CASP9 is now in full swing and we need your help! We are being overwhelmed with targets and need as much CPU power as possible!
I just got this from the organizers:
Subject: CASP update - May 7
First week of CASP9 prediction season is over. We have released 14 targets. The vast majority of them were easy TBM targets. Next week you will find some harder targets in the human prediction category.
As of today, we have 125 groups (predominantly servers at this early stage) contributing models to the Prediction Center. You can always find the latest CASP statistics at http://predictioncenter.org/casp9/numbers.cgi .
If you are interested in following the prediction season as it happens, the above web site is a good source of information.
We are absolutely delighted by the recent increase in the total throughput of rosetta@home, which could not come at a more critical time! we are having to make very difficult choices between CASP9 structure prediction calculations and the next generation of pathogen inhibiting proteins building on our success with the flu virus inhibitor, and the new contributions of computer power many of you are making are helping immensely. Thank you very much!
We have now confirmed the tight binding of our designed Spanish Flu inhibitor to the flu virus using multiple different methods (it is always good to be totally certain with exciting results like these!). For those of you with some chemistry background, the binding constant is about 20nM.
With collaborators at Scripps research institute we are now trying to determine the structure of the designed complex between the inhibitor and the virus by x-ray crystallography (to see whether binding is as in the design model). With the tight binding confirmed, we are now starting to investigate whether the designed protein prevents the virus from infecting cells.
A manuscript describing the results on FoldIt, which many of you contributed to, was just accepted for publication in Nature. The idea for FoldIt came from rosetta@home participants who posted on the message boards about wanting to be able to guide the course of the folding trajectory. Please keep letting us know your thoughts and suggestions!
Rosetta@home has now been directly responsible or closely associated with two papers in Science (one on enzyme design, one on new approaches for structure determination) and two papers in Nature (this one on Foldit, and one last year on endonuclease design for gene therapy) in the last 9 months. This kind of impact at the forefront of scientific research is I think a first for volunteeer computing, and perhaps the strongest indication to date of the power and value of volunteer computing for pushing forward the boundaries of scientific understanding.
Thank you all for your invaluable contributions to our collective efforts!
The most recent issue of Science magazine has our paper on the use of Rosetta to design a new carbon-carbon bond forming enzyme, along with a commentary. This paper has attracted a lot of attention in the press. Thank you all for your contributions to this work and to our ability to move forward with designing enzymes and other proteins that will hopefully be of use to society in not too long.
There have been exciting developments in our work to develop general methods for designing proteins that can bind to and block the activity of any desired target protein. There are now three targets for which we have designed and experimentally validated binders: a widely used "model" protein called lysozyme, a protein involved in biosynthesis in the bacteria that causes tuberculosis, and a key protein on the surface of the H1N1 flu virus. In the flu case, our collaborators have just solved the structure of our designed protein bound to the virus protein and it is amazingly close to our computational design model.
Now that the methods seem to be working pretty well, we are thinking more about applications. One of these is to make cheaper and more robust diagnostics kits. We are now collaborating with groups interested in developing low cost diagnostics for the flu virus (and other pathogens). our designed proteins are very easy to make in large quantities, and our collaborators are going to test how well they work in place of more expensive and less stable antibody molecules in diagnostic kits.
In the past I've described a brand new approach using Rosetta to design vaccines for which there are not effective current vaccination treatments. HIV, for example, has turned out to be fiendishly effective at evading the immune system, and as you probably know, despite much work there is no really good vaccine. In collaboration with other groups, Rosetta has been used to design small proteins that present "Achilles heel" regions of the virus to the immune system to stimulate the production of antibodies which recognize these regions. The first papers on this have now been published and, while the designed proteins have not yet elicited strongly neutralizing responses, there is considerable excitement over this new approach. You can read about it at
The Gates foundation has just awarded $1,000,000 to a collaborative project to develop specific enzymes that cut within HIV DNA in cells into which the virus has integrated:
One of the many nasty things about HIV is that it can reside for a long time in a latent state where it can't be detected by the immune system. If we can generate enzymes that cut up the virus when it is hidden inside a genome, its hiding place will be destroyed. Keith Jerome's lab at the UW is developing methods for delivering enzymes to possibly HIV infected cells, and a graduate student working between our groups is using Rosetta to design endonucleases which cut within the HIV DNA sequence. I'll keep you posted on the progress of this exciting project!
First, I would like to thank everybody for bearing with us while we recovered from a critical server hardware failure. Over the next month or two we will be installing more powerful and more robust hardware so hopefully this will not happen again.
Second, I'd like to tell you briefly about another exciting success with Rosetta. When structural biologists work to solve protein structures by putting protein crystals into x-ray beams and recording the diffraction pattern, they only have half of the necessary information. The other half (the "phase" information) can be quite difficult to obtain. In the past six months, we've collected about 15 cases where protein crystallographers were stuck and could not solve the structure. Using Rosetta, we built models for these proteins of sufficient quality to allow the inference of the missing information and subsequently the solution of these structures. This opens the door to a much easier way of solving challenging protein structures, and there are lots of scientists excited about using the new method. The new method is described in a manuscript which will likely appear soon in Nature magazine.
Again, thank you for sticking with rosetta@home during our recent server problems -- there is a lot of exciting scientific research that is only possible because of your contributions!
The new hardware is now being installed, and we are very happy to put the server failures behind us-hopefully we will have no outages this severe again for a long time!
The manuscript I described in my last post on solving crystal structures using Rosetta has now been formally accepted for publication in Nature; the paper will be in an issue on newstands in a month or two.
In a previous post I described the design of small proteins which bind to and block the function of the key surface protein on the influenza virus, called the haemagluttinin (I can never spell that right!). We are very excited about the possibility of making more proteins that bind to the various strains of the virus that could serve as anti flu drugs (this would only be for very acute infections as you probably wouldn't want to take a dose of these too many times) and are actively working on this. Meanwhile, a manuscript describing the design of the first proteins and how they block the haemaglutinin from the Spanish Flu influenza virus has just been accepted as a full research article in Science magazine. We are excited (and nervous) because we've never been this close to making an actual drug before (as I've explained before, most of what we do is directed more at basic understanding than actual drug development). Still, of course, it is a long road (clinical trials, etc if we get that far) to get something to the point it can be used as a drug. I'll keep you posted as we move along with this.
The paper on the Rosetta method which allows determination of the structures of a large class of proteins using limited crystallography data has now been published in Nature magazine. Thanks to all of you for making this work possible!
Graduate student Shawn Yu is now posting on current Rosetta@home efforts to design inhibitors for viruses that cause disease in the "Design of Protein Interactions" thread on the Science message boards. Take a look if you are interested; he is happy to answer questions in the thread as well.
This week's issue of Science magazine features an article on the use of Rosetta@Home to design novel proteins which bind tightly to the Spanish Flu (H1N1) Influenza Virus. The paper shows that the experimentally determined atomic structure of the complex between one of the designed proteins and the virus is precisely as in the computer model. The designed proteins block the function of the flu surface protein in biochemical tests, and we are guardedly optimistic that the designs will block flu infection. This is an important milestone for computational protein design (and for distributed computing)--the first atomic level accuracy design of a high affinity protein-protein interface, and the designed proteins are exciting leads for new flu therapeutics. In the next few months, we will be using Rosetta@Home to design proteins that bind tightly and hopefully block other pathogens which cause disease. Thanks to all Rosetta@home users for their invaluable contributions to this research!!
(if you want to learn more, the Science web site has a podcast discussing the work:
A recent issue of Nature describes an exciting approach we are taking with collaborators to fight Malaria. The title of the paper is "A synthetic homing endonuclease-based gene drive system in the human malaria mosquito" and the PDF is available at my lab web site. The idea is to use enzymes which cut within critical genes in mosquitos to greatly reduce the number of malaria parasite infected mosquitos. There are still many issues that must be overcome for this strategy to be used against malaria in the real world, but this paper is an important first proof of concept of the strategy.
This week's issue of Nature magazine has an exciting article (http://www.nature.com/nature/journal/vaop/ncurrent/full/nature10154.html) describing work we are doing with collaborators using Rosetta to design a new class of inhibitors of amyloid fibril formation. Amyloid fibrils have been implicated in Alzheimer's and many other diseases. The designed peptides are not suitable for use as actual therapeutics in their present form, but hopefully will help lead the way to effective drugs.
Today's issue of Nature Structural Biology reports the determination of the structure of a protein by FoldIt players. This is exciting because it is perhaps the first example of a long standing scientific problem solved by non-scientists. You might read about this in your newspaper; here is a report that does a good job in explaining how FoldIt came out of Rosetta@home:
A recent issue of Nature describes an exciting result from Rosetta@home in collaboration with the NMR spectroscopy laboratory of Lewis Kay in Toronto. Like almost all machines, proteins in order to carry out their functions have to move (change their conformation somewhat) but it has been extremely difficult to determine what these conformational changes are. Lewis Kay's group has developed new methods for getting experimental information on the higher energy very shortlived conformations proteins visit while carrying out their functions. This data is not sufficient to determine the structure of these "excited state" conformations using conventional methods. However, as the paper shows, we can use these experimental data to guide Rosetta and Rosetta@home structure calculations, and produce models of these states. We went one step further than this in the paper by using Rosetta design calculations to stabilize the excited state, and subsequent experiments confirmed the validity of the model. This combination of experimental NMR data, Rosetta structure calculations, and Rosetta design should be very powerful in understanding how proteins carry out their functions.
Today's issue of Science magazine describes an exciting new approach to HIV vaccine design using Rosetta. In contrast with other viruses such as polio and influenza, inactivated HIV or HIV proteins have not worked as vaccines, and hence as you know there is currently no effective HIV vaccine. Our approach to vaccine design is to take the bits of the HIV surface protein that people make antibodies to, and using Rosetta graft them onto small stable scaffolds that can be made in large quantities and potentially could be useful as vaccines. We've shown earlier that this can be done straightforwardly with Rosetta if the bits of the HIV protein are contiguous along the sequence, but it is much harder if the antibody recognizes multiple bits close in three dimensions but far in sequence. In this paper we show how such "discontinuous" epitipes can be transferred from HIV gp120 to a simple scaffold protein. More work will be required to determine whether this or other vaccine candidates designed using this approach will be effective as HIV vaccines-let us all hope so!!
In response to requests from many of you, we will be posting descriptions of the many scientific problems currently being tackled with Rosetta@Home on the Science message boards in the next couple of weeks--stay tuned! I also want to describe a new research direction we are now embarking on aimed at future cancer therapies. There are a small set of proteins which are frequently found at much higher levels than normal on the surface of cancer cells. We are starting to design small proteins which bind tightly to these tumor cell markers. If we are successful, we have collaborators who will be testing these proteins for their ability to target cancer cell killing agents to the tumors.
Last year we described in Science magazine the design of a new enzyme which catalyzes a chemical reaction called the Diels Alder reaction involving the formation of two carbon-carbon bonds. This reaction is interesting because no natural enzymes are known to catalyze the reaction. However, it wasn't a very good enzyme, and we asked FoldIt players to try to improve it. As described in Nature Biotechnology this month, remarkably FoldIt players were able to make the designed enzyme 20 times faster by inserting a completely new loop which helps the enzyme bind the chemicals it links together. The combination of Rosetta@Home and FoldIt is turning out to be powerful indeed for solving challenging problems in biomedicine!
In the last two months we believe we have made quite a breakthrough in structure prediction, and are excited to test the new method in CASP10. We need your help though--we are now testing many aspects of the new approach and are seriously limited by available CPU cycles. There are now so many flu inhibitor design and structure prediction jobs queued up on Rosetta@Home that there is an eight day wait before they are getting sent out to you. This would be a great time to temporarily increase Rosetta@Home's share on your computers and/or recruit new users--we need all the help we can get! thanks! David
I've described in the past our work using Rosetta and Rosetta@Home to create new enzyme catalysts. In Nature Chemical Biology last month we describe the design of an enzyme which destroys organophosphate
nerve agents and pesticides. These compounds kill by blocking key enzymes, and our designed enzyme eliminates this toxicity. This illustrates how Rosetta@Home enzyme design work can help to solve current problems, including man-made problems.
I have just been told the very good news that Rosetta@home will be the first project of the BOINC pentathlon, and would like to thank all of the participating teams. I also just learned from the discussion thread that Rosetta@home will be the project of the month for BOINC synergy-this is more excellent news!!
Your increased contributions to rosetta@home could not come at a better time! We've been testing our improved structure prediction methodology in a recently started challenge called CAMEO. For most of the targets, the Rosetta@home models are extremely good, but for a minority of targets the predictions are not good at all. We've now tracked down the source of these failures and it is what we are calling "workunit starvation"; in the limited amount of time the Rosetta server has to produce models (2-3 days) in these cases very few models were made-this happens because many targets are being run on the server so that only a fraction of your cpu power is focused on any one target. while we are working to fix this internally, by far the best solution is to have more total CPU throughput so each target gets more models.
You can follow how we are doing at http://www.cameo3d.org/. You will see that Robetta is one of the few servers whose name is not kept secret-this is because Rosetta is a public project. Our server receives targets from CAMEO and soon CASP, sends the required calculations out to your computers through Rosetta@home, and then processes the returned results and submits the lowest energy models.
We are excited that the workunit starvation problem may go away through your increased efforts for Rosetta@home. Thanks!!!
A big THANK YOU to all of you who have scaled up your contributions to Rosetta@Home-this is a record level of computing power for us and is super well timed. THANKS!!!
Many common materials such as silk and wool are made out of regular repeating arrays of proteins, and symmetric protein arrays make up the coats of viruses and many other assemblies inside cells. The ability to robustly design self assembling materials made out of proteins would have huge numbers of applications-the naturally occurring assemblies are useful, but imagine if we could make custom materials for 21st century problems. In this weeks Science magazine, we describe the use of Rosetta to design self assembling protein nano structures with very high accuracy. We are now attempting to create many different types of symmetric materials, and you will be seeing more symmetric calculations on your rosetta@home screen server. Thank you for making possible this completely new approach to nanotechnology!
A recent paper in Nature Biotechnology describes how we have combined computational protein design with the high throughput DNA sequencing methods developed for sequencing the human genome to generate potent influenza virus inhibitors. These designed proteins block infection by the flu virus in cell culture experiments, and they are now going through the (quite lengthy) process of being developed as possible anti-flu drugs.
We are now testing the latest batch of novel designed proteins that you have helped us create in our brand new Molecular Engineering laboratory at the UW. You can see pictures of the space where the rosetta@home computed designs are being experimentally tested in a recent newspaper article:
The native structures are slowly being released for CASP10 targets; all of them will be available by the end of November. In the meantime, you can look at the results of a much larger scale test of prediction methods called CAMEO. CAMEO takes newly solved protein structure before they are published, and sends the amino acid sequences out to structure prediction servers. This happens every week, so it is great to assess new methods as they are being developed. You can look at the results, as well as get more information about CAMEO, at
The best number to compare is the "Average accuracy (all targets)" as some servers only model the easy ones. The good thing about CAMEO is that there are many more test cases than CASP, and also that results are released each week so we can see what is working well and what needs to be improved. You will see that ROBETTA, which is now using some of your computing resources, is doing pretty well recently; before this we had problems with some targets not getting enough work units before the server deadline.
I have exciting news. We and the University of Washington are starting up a new Institute for Protein Design to design new proteins to address current challenges in medicine, energy, and other areas. You can learn more about the institute at http://depts.washington.edu/ipd/. Rosetta@home is and will continue to be a critical part of our efforts. For every new potential protein therapeutic we design, we use Rosetta@home to test whether it will actually fold into the desired structure. And we need help! We have quite a backlog of exciting new designed proteins to test on Rosetta@home because we are designing proteins for quite a range of problems-new anti flu proteins, anti-cancer proteins, and new materials--and it takes 3000-5000 work units to test each one. This Rosetta@home testing is becoming the slow step in the whole design process, often taking over 10 days to complete. So please tell your friends and relations to join us!
A generous donor has provide funds which we want to use to invite 5-10 Rosetta@home participants to visit the Institute and see what we are trying to accomplish first hand. More on this in my next post.
With your help, we have made an exciting breakthrough in protein design that is reported in a research article titled "Principles for designing ideal protein structures" in the journal Nature today. You can read about it at
In this paper, we describe general principles for creating new proteins from scratch. The new Institute for Protein Design is using these principles to design new proteins to treat disease.
Rosetta@home was absolutely critical to this work as described in the news article; Figure 3 in the paper shows how all of your contributions were used to test designed sequences to see if they folded up to the right structure. Most of the work units we are sending out on Rosetta@home these days are for exactly these kind of tests on the new proteins we are designing--this is absolutely critical to the research and to the development of new therapeutic and other functions. Thank you again for all of your contributions!
We would like to acknowledge the Rosetta@Home participants who found the lowest energy structures for Nobu and Rie's designed proteins:
Fold-I : Aalelan (United States)
Fold-II : Jef (United States)
Fold-III : georgebg (Bulgaria)
Fold-IV: medvjet009(Czech Republic)
Fold-V : _2e_ Russia.
See Nobu's message board thread on "Principles for designing ideal protein structures" (http://boinc.bakerlab.org/rosetta/forum_thread.php?id=6113) for more information including a figure illustrating the critical role played by Rosetta@home in this work. And check out the latest on slashdot:
This and other publications from the lab are available at depts.washington.edu/bakerpg
Thanks again to everybody!!
The CASP10 meeting just finished and all the results are on line so you can see what all your contributions made possible! Ray has posted a great summary of the results in the CASP10 thread on the science message boards. Overall, Rosetta@home was top or near top in most categories. I hate to embarrass David Kim who created RosettaHome and has kept it going, but his contact guided predictions were the highlight of CASP10 as they were vastly better than those of any other group. You can see this at
David's predictions are the black lines, those of other groups are in orange, better models stay below the rest of the pack.
Thanks to all of you who contributed to CASP10!!
We have learned to design a new class of proteins which could be useful both as drugs and in sensors. As I've explained before, most drugs are small molecules with fewer than 50 atoms. There are many drugs, such as blood thinning agents, which are very dangerous if given in too large doses. We have succeeded in designing proteins which bind to specific small molecules very tightly. These proteins could be used as antidotes in case of overdose with the target small molecule-for example we've designed a protein which could be useful to treat toxicity due to overdose of the drug digoxin used to treat heart disease. With collaborators, we are working to use these designed proteins to detect levels of the target small molecules in the blood or in the environment.
We have discovered how to make several new classes of protein structures! Rosetta@home has been absolutely critical in this work: when we design a sequence to fold into a new structure, the last thing we do before ordering a synthetic gene so we can make the protein in the laboratory is to send it out to you to predict the structure-if it folds to the structure we designed, we go ahead with it, but if you find that the lowest energy state is a different structure we go back to the drawing board. Our success rate in making brand new structures is far higher than I or anybody else ever expected, and the reason the success rate is so high is that your calculations provide a very stringent test of whether the designed sequence will actually fold the way it is supposed to. In the next few weeks I and other scientists here will describe to you the new classes of proteins we are making, and the many applications they will be useful for. Thank you for your absolutely essential contributions to this newly emerging scientific field!
Our new Institute for Protein Design is making considerable progress as you can see at http://depts.washington.edu/ipd/. we are now using Rosetta@home to rigorously evaluate all computer-based designs before we create synthetic genes to make the proteins in the laboratory. this is dramatically increasing our success rate at designing proteins with new functions. your contributions continue to be absolutely invaluable!
An article mentioning Rosetta@Home recently appeared in the Globe and Mail:
There has been very exciting recent progress in designing vaccines and small molecule binding proteins using Rosetta that is described in two recent papers in Nature. These and other recent advances are described in the new Rosetta@Home Research Updates thread. It was suggested there that we send out a monthly email newsletter describing recent progress--we haven't done this before to avoid clogging everybody's inboxes but we certainly could if there is interest.
We have recently made great progress in designing self assembling materials from proteins and in designing proteins which selectively kill tumor cells. These efforts have benefited tremendously from Rosetta@Home! News releases on these advances are at
We just published a paper in Nature that depended critically on all of your contributions! You can get the pdf for this paper on our website; you can also get pdfs of the many other papers we've published in the last couple of years that relied heavily on rosetta@home. Here is the link to the recent Nature paper:
The results on the flu neutralizing protein you helped us design have now been published. You can get the paper, like all of our papers, from our lab web site, and read what journalists are saying at
I recommend listening to graduate student Yang Hsia's podcast on designing protein footballs which you can find on the Nature web site this week to go along with his paper. (see Ratika's post for the link if you can't find it). Thank you all again for all of your contributions to our research-we couldn't do it without you!
We all collectively made the cover of the July 22nd Science-check it out! This same issue also has a news feature on our work, and an article on designed icosohedral cages made from two different designed protein building blocks. For more information and links to the papers, see Ratika's post in her thread.
A link to "Ratika's post" for you, where you can also find links to a video explanation of the process.
Rosetta Moderator: Mod.Sense
Hi Everybody!
this has been a good week with papers in this and last weeks Science magazine. your contributions were essential for both breakthroughs! here is some of the press you might find interesting:
thank you again for your invaluable contributions to this research!!
NOVA recently featured some of the work that all of you are contributing to:
http://www.pbs.org/wgbh/nova/physics/origami-revolution.html utm_medium=novasocial&utm_campaign=nova_2016&linkId=34331189 (the 8 minute segment on our work starts at 20:30)
The Economist also had an article on the work you are contributing to:
Your contributions are highlighted particularly clearly in the Geekwire article:
which is titled "Big data (and volunteers) help scientists solve hundreds of protein puzzles"
Message boards :
Rosetta@home Science :
David Baker's Rosetta@home journal


text:
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subset: commoncrawl


text:
Archdiocese of Chicago
The Office for Immigrant Affairs & Immigration Education was created by the Archdiocese of Chicago in July 2009 to combine the efforts of education and advocacy for comprehensive, compassionate immigration reform with our new Immigrant-to-Immigrant Ministry (e.g., Pastoral Migratoria).
In late June, the United States Senate, through a bi-partisan collaboration, passed their version of a comprehensive immigration bill. Speaking on behalf of the US Conference of Catholic Bishops, Archbishop Jose Gomez of Los Angeles reaffirmed that this was commendable, but that there is still work to do.1 He is right. In the coming weeks the House of Representatives will return from their summer recess bearing the responsibility for proposing and debating their own immigration bill.
Understanding the role of migration in our faith tradition, and seeing the implications that migration has for living a dignified life, the Church has stood on the side of the immigrant community during the journey for comprehensive immigration reform. In the document "Strangers No Longer: Together on the Journey of Hope," the bishops from the US and Mexico presented a guideline for how political leaders and people of faith and good will should act when reflecting on this debate:
We seek to measure the interest of all parties in the migration phenomenon against the guidelines of Catholic social teaching and to offer a moral framework for embracing, not rejecting, the reality of migration…We invite Catholics and persons of good will… to exercise their faith and to use their resources and gifts to truly welcome the stranger amongst us (cf. Mt 25:35) (7)2
In response to calls like this, the Archdiocese of Chicago and the Office of Immigrant Affairs are introducing a "40-Days of Prayer, Fasting and Action for Congress." This campaign, developed from a planning meeting in July amongst 120 parishioners from 32 parishes in the Archdiocese, seeks to offer the time and space for unity amongst the church to pray, reflect, and act in solidarity with our immigrant brothers and sisters. Parishes throughout the Archdiocese have been committing themselves to prayer, fasting, and action of their choosing during this period, and we invite all people of faith and good will to engage their communities and join us. You can either talk to your parish to see what actions they have committed to, or you can go to www.archchicago.org/Immigration/ to view suggestions that were formulated during the July meeting.
The campaign will start at the Archdiocesan level on Thursday, August 15, with a pilgrimage and mass in conjunction with the Our Lady of Mercy parish community. The pilgrimage will begin at Our Lady of Mercy Church (4432 N. Troy St., Chicago) at 6:00 p.m. We will walk less than a mile to Rosana Park (Sacramento and Ainslie Streets in Chicago) where we will celebrate mass starting around 6:45 p.m. All are invited! We will end our campaign with a pilgrimage on October 12. Please look out for more information as the date nears.
To learn more about the Bishops' stance, please visit: www.justiceforimmigrants.org/bishops-call.shtml. The passage of the Senate bill is a victory for advocates for immigrant justice, but our prayers and voices are needed to ensure that comprehensive immigration reform will be made into law.
2 www.usccb.org/issues-and-action/human-life-and-dignity/immigration/strangers-no-longer-together-on-the-journey-of-hope.cfm
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Monday, July 11, 2016
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By Christopher Cox
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2014/04/08 - 20:37 •
VOICES OF THE REVOLUTION: Occupation Memoirs of Servicemen Relocated from Crimea.
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Charcoal is one of the by-products of fire. It is almost pure carbon, and at first sight may be considered an unlikely source of information about past life on the planet. However, when plants are charred by fires many of their very finest anatomical details are not affected. Just as importantly, charcoal is often subsequently left virtually unaffected by the fossilization process, as it is relatively chemically inert. As long as this brittle material is not crushed, beautiful anatomical detail can be seen microscopically, even in specimens as much as 419 million years old. This incredible preservation is not just restricted to wood but can also affect any other plant organ that was charred, no matter what its size or delicacy. Many of the earliest land plant fossils, often measuring just a few millimeters in height, are known in detail because they were preserved as charcoal. Similarly, much of our knowledge of early angiosperm evolution and diversification during the Cretaceous comes from the charcoalification of reproductive structures, even flowers.
SEM Image of Cretaceous flower from Allon, Georgia, USA preserved as charcoal
Ancient charcoal can tell us both about the nature of ancient fire itself, including the minimum temperature any given fire may have reached, as well as the plants being burned. However, research by Ian Glasspool (Field Museum of Natural History) and Andrew Scott (Royal Holloway University of London) also suggests that ancient charcoal in coal deposits can be used to predict past concentrations of atmospheric oxygen. At present the atmosphere is composed of about 21% oxygen but this level was suspected to have been much higher during the past. These levels are of more than just passing interest; relatively high concentrations of atmospheric oxygen on Earth have strongly impacted the evolution of life with links suggested to the evolution of tetrapods, gigantism in sauropods, placental mammals, insect gigantism, powered flight in both birds and insects and to the Permo-Triassic mass extinction.
Predictions of Phanerozoic atmospheric oxygen concentration based on the work of
Bergman et al., 2004, Berner, 2009 and Glasspool and Scott 2010.
The work by Glasspool and Scott exploits the correlation between atmospheric oxygen concentration and flammability to make predictions about the past based on the abundance of charcoal. At low levels (around 15%) fires are unlikely ever to have propagated, no matter how dry the plants; but at oxygen levels of about 30% even wet plants can burn and fires would become rampant producing large volumes of charcoal. The charcoal data indicates that about 400-390 million years ago, during the Middle Devonian, atmospheric oxygen levels were very low, well below modern levels. However, the concentration then rose rapidly over a 30 million year interval following the growth of the Mid-Late Devonian forests and from the Mississippian remained at levels above 26% until the Mesozoic. Phanerozoic atmospheric oxygen levels peaked at about 29% during the Early Permian and remained relatively high until at least the last 2.8 million years of the Permian. A pronounced collapse in atmospheric oxygen concentration occurred following the Permo-Triassic extinction, but this decline appears to have followed rather than driven the extinction. The Mesozoic appears to have experienced large amplitude cyclical fluctuations in atmospheric oxygen concentration throughout the Triassic and Jurassic, levels then rising throughout the Cretaceous until reaching another peak during about 100 million years ago. From this point onwards oxygen levels declined until they appear to have reached relative stability at about 21-22% over the last 40 million years.


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Beautiful Condo in Hollywood
Size1400 ft²
Floor No.2
- Kitchen
- Air conditioning
- Washer/dryer
- Parking available
- Internet/WiFi
- Balcony/terrace
- Towels
Accommodation summary
|Sunset Blvd, 90028 Los Angeles, United States
|Property type
|Property ID
|Acceptance rate
|Response time
|A few hours
|Calendar updated
|A week ago
Area Info
The condo is just minutes away from the famed Sunset/Vine and Hollywood/Highland where you can walk the "Walk of Fame", experience the foot and hand prints of all of your favorite stars of past and present at the "Chinese Theater". You want nightlife... you have it! Just steps away for Hollywood's most famous clubs and bars. You will not go hungry too for there are several restaurants within walking distance as well as a 24hr convenient store right across the street. Post Office is also across the street!!! You really could not be in a better location!
House rulesNo parties allowed. ABSOLUTELY NO SMOKING INSIDE APARTMENT! A 250 € fee will incur for smoking.
A $300 Refundable Security Deposit will be collect at check in for damages and will be returned at the end of stay.
|Weekly rate for up to 5 guests
|Monthly rate for up to 5 guests
|Price for > 5 guests
|$ 35 AU per guest/night extra
|Check-in after
|Check-in before
|On arrangement
|Check-out before
|Cancellation Policy
Reviews of this property
This was my first experience with Wimdu and immediately a hit. Booking and contact with John in the run has worked out great. John's brother was waiting for us in the apartment and very friendly welcome. The apartment is spacious on two levels, great kitchen, living room, dining room, 2 bedrooms, 2 bathrooms, all in good condition and clean. Free WIFI works very well. But the best part is the location: walking distance to Sunset Boulevard and the nearest metro station (1 stop to Universal Studios)! Apartment is ideal for families.
Dies war meine erste Erfahrung mit WIMDU und gleich ein Volltreffer. Buchung und Kontakt mit John im Vorfeld hat super geklappt. Johns Bruder hat uns in der Wohnung erwartet und sehr freundlich empfangen. Die Wohnung ist großzügig auf zwei Ebenen angelegt, tolle Küche, Wohnzimmer, Esszimmer, 2 Schlafzimmer, 2 Badzimmer, alles in gutem Zustand und sauber. Gratis WIFI funktioniert sehr gut. Das beste ist aber die Lage: wenige Gehminuten zum Sunset Boulevard und zur nächsten Metrostation (1 Station zu den Universalstudios)! Wohnung ist ideal auch für Familien geeignet.
We've just returned from LA, having spent the week at John's apartment. Perfectly central location, our own parking bay and a really well equipped kitchen. The apartment was spotless and also spacious. Two large bedrooms with each having their own en-suite, and a separate loo downstairs. Also a fantastic washing machine and drier available, we came home with clean clothes! Both bedrooms also have ceiling fans & there is air-conditioning. Honestly, hand over heart, we can vouch for this Condo. Comfy sofas & hot showers, 7 eleven across the road, restaurants up and down Sunset Blvd. John, our host was also lovely. We'll visit again!!
We found the location excellent. JJ was good to deal with. We had a little bit of confusion locating the property but once settled we found it suitable for our family of 5. It is in easy distance to walk to Hollywood blvd. There is a 7/11 across the road and a larger grocery shop near by. We found the place clean and the kitchen had every gadget known to man. Thanks JJ. We enjoyed our stay and would recommend it to others.
The apartment is super well located, very clean. We loved our week spent there. There is a parking privatized local shops 10 metered, the apartment is near the main roads north of LA. John was very nice. I highly recommend this apartment and I will gladly. Thank you very much John.
L'appartement est hyper bien située, est très propre. Nous avons beaucoup aimé notre semaine passé la bas. Il y a une place de parking privatisé, des commerces de proximité à 10 métrés et l'appartement est prés des artères principales de north LA. John a été très sympa. Je recommande fortement cette appartement et j'y retournerai volontier. Merci beaucoup à John.
Very nice apartment. Well located, a few minutes from Hollywood Boulevard. 2 bedrooms each with a bathroom and toilet. Beautiful living space, large kitchen and laundry room for washing if necessary Important to note, a parking space is available in the apartment which is a plus. I recommend this address
Très bel appartement. Bien situé, a quelques minutes d'Hollywood boulevard.
2 chambres équipées chacune d'une salle de bain et toilettes.
Bel espace de vie, grande cuisine et buanderie pour laver le linge si besoin
Important a signaler, une place de parking est disponible avec l'appartement ce qui est un plus.
Je recommande cette adresse
Home again. We were in a wonderful apartment in LA.We felt very comfortable and would definitely book again on a next trip. Thanks, John!
Bye, bart
The apartment has a good location, it is walking on hollywood bulevard in few minutes. Without a car you are in a fix but to los angeles. The apartment is large and you have everything you need. Would recommend it to all. Thanks john we had a great stay!
Die wohnung hat eine gute lage, man ist zu fuss in paar minuten am hollywood bulevard. Ohne auto ist man jedoch aufgeschmissen in los angeles. Die wohnung ist gross und man hat alles was man braucht.
Würde es jedem weiterempfehlen.
Thanks john we had a great stay!
The appartement at Sunset Blvd. is very nice. It has plenty of room, is very well taken care of and is located near Hollywood Blvd and Sunset Blvd. It also has its own parking space. We have enjoyed our three night stay.
Beautiful and large apartment in a great location! Walk of Fame / Hollywood Blvd within walking distance. Very friendly and trustworthy host! Keys without a problem. We can recommend the apartment and the host! Thanks John :))
Schöne und große Wohnung in super Lage! Walk of Fame / Hollywood Blvd fußläufig zu erreichen. Sehr freundlicher und vertrauenswürdiger Gastgeber! Schlüsselübergabe problemlos verlaufen. Wir können die Wohnung und den Gastgeber empfehlen! Thanks John :))
Apartment is well (depending on the tour los angeles), very nice We were particularly affected by the kindness and TRUST (refused bail ....) granted by the host I relouerai this person certainly in the future and call again for your services to another location in a word: Perfect
Bel appartement bien situe, ( en fonction de la visite de los angeles ), très agréable
Nous avons été particulièrement touchés par la gentillesse et la CONFIANCE ( a refusé la caution....) accordée par l'hôte
Je relouerai à cette personne certainement à l'avenir et repasserai par vos services pour une autre location
En un mot : TRES SATISFAIT
- Quality assured accommodation
- Every host is verified by telephone
- Secure payment via SSL encryption


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Just choose your country with our new guide!
Interpower is the premier supplier of power system components worldwide. Founded in California in 1975, Bob Wersen, President of Interpower, has made it easy for customers to design, build, and maintain products for worldwide markets ever since. Now based in Oskaloosa, Iowa, Interpower manufactures cord sets and power cords in the United States for the North American and international markets and has an office in the United Kingdom.
All of our products go through safety tests and meet national and international standards. Each year you can find us at trade shows, including a virtual show online, where you can browse our quality products. To see a list of our upcoming trade shows, see our trade show schedule. We would be delighted to meet with you and highlight our products.
In addition to browsing our products available to order, check out our Product Design Library where you can watch webcasts and find quality testing measures. Our webcasts include topics such as national power mains and what engineers should know about designing international products. You can always find out what's new in cord sets and power cords for the North American and International markets in our blog.
You will be delighted by our quality products and how fast and easy it is to order and start receiving our power system components. You will be able to unpack and use our products immediately. We are your one-stop shop for all your power component needs.
We make it fast and easy to order North American and international power cords, including hospital/medical-grade power cords that you can find on our hospital-grade products page. Order online or call us today. We offer no minimum order or dollar requirements, a 1-week U.S. manufacturing lead-time on non-stock Interpower products, and same day shipments available on in-stock products (4 million parts in stock!).
Contact Interpower today!


text: I actually did not go to the doc. I talked to the Great Physician. Also, We talked to a natural health person nearby and used some EOs that they recommended. Really what did the trick. Truly knocked the crud out of me. I feel like a new person. I do to even have a fever. So EOs work on humans and bees!


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Wednesday, June 24
8 a.m. to noon, GED instruction and college preparation, Anderson Community Education building, 219 E. Woodford St.
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Coded word for a girl to her ex which translated means: "I've been cheating on you with a fat ugly stoner that works at Fry's because I'm jealous that you bought some girl a present and she's prettier than me and she's a gosh dawn cawlidge gurl and I ain't."
Or at least what I think it means, now.
Or at least what I think it means, now.
Angie told me she was "Taking a break from guys" but her Myspace comments with that "Creepy guy" that wanted to be a girl for Halloween have shown me the truth.


text:
Teaching includes lectures, seminars, workshops, team project work, literature reviews. Independent research is encouraged.
Assessment includes essays, presentations,group work, exams, portfolios, reflective learning journals and final-year project (a dissertation, collaborative policy-orientated research or report based on a work placement).
The number of learning hours for each module is determined by its credit weighting. For example, for a 30-credit module there would be 300 learning hours. This would be divided into contact hours (eg time spent with your core course team) and independent learning hours (eg time spent on research with or without technical support).
Coursework is designed to be achieved within the set amount of learning hours for each module and is appropriate to the level of study. We encourage a professional work ethic, which includes how to manage your time. A range of additional support is available to students who require it.
Our courses are carefully constructed to allow you to build knowledge and skills progressively during your degree programme.
We constantly update our curriculum to ensure that it covers the latest developments in your subject area, including the research and professional experience that your tutors bring to the course.
Our course teams also draw on the wealth of experience provided by our professional contacts and highly successful alumni who feed into the design of our courses and provide masterclasses and workshops to enrich your learning.
Our courses take a progressive approach to help develop your academic skills through the modules you study.
Our Academic Skills Centres also provide one-to-one support and advice on the techniques you need to be a successful student including:
During your degree you will develop the independence, creativity and excellent communication skills that we know employers look for in successful graduates.
Assignments are designed not just to test what you know, but to help you develop your knowledge, skills and confidence.
Because we want you to reach your full potential in every assignment, we build in opportunities for practice and 'feed forward' on assessment tasks so that you will know what you need to do to perform at your best when you submit your work.
When we return your work, we give you clear feedback that will show you what you need to work on next time. You'll have the opportunity to discuss the comments on your work one-to-one with your lecturers and your personal tutor.
When you arrive, we'll introduce you to your personal tutor – the member of academic staff who will keep a particular eye on your progress throughout your time at Kingston University (and after you graduate) and who will show you how to make the best use of all the help and resources that we offer at Kingston University.
Your tutor will give you academic guidance and will make sure that you know how to access our other support services if you need them.
A programme specification is a summary of the main features of a programme and provides details of the intended learning outcomes for students. It details the teaching, learning and assessment methods, including the structure of the programme.
Admissions team
This course is taught at Penrhyn Road
Admissions team
This course is taught at Penrhyn Road


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I bought the new Sigma 17-70mm F2.8-4.5 DC MACRO and this really is a great lens!
The only gripe I have with it is focussing in low light... it just struggles so badly but apart from that it's a winner. Here's a pic recently taken with this amazing lens.
Has anyone else used this lens and what are your thoughts?
Heinz Schmidt
Sigma 17-70mm F2.8-4.5 Dc Macro
Started by hedward, May 16 2006 10:34 AM
2 replies to this topic
Posted 16 May 2006 - 10:34 AM
Posted 29 August 2006 - 10:36 PM
I have this lens as my main work lens. For what it is it does a great job. Its not a great macro lens but as an all purpose zoom its great.
Posted 12 March 2007 - 05:43 PM
QUOTE (Cemalina @ Aug 29 2006, 02:36 PM) <{POST_SNAPBACK}>
I have this lens as my main work lens. For what it is it does a great job. Its not a great macro lens but as an all purpose zoom its great.
This has turned into my main walk-around lens. I honestly thought I would want to go to a 17-40 or similar L lens, but this little lens is so versatile, I think I will miss some of the features if I switch.
Things I like:
-not true macro, but fills many close up needs very well
-minimum focus distance is wonderful
-extremely sharp right from the box - fast and quiet AF
-f2.8 at wide has been fine for me - not useful zoomed in low light, but neither is a 17-40 L.
I have tried but can't find better price/performance value - I also carry the 70-200 ex dg 2.8 which is stellar. Would like to see Sigma do a ex dg version of this lens.
Any suggestions for a comparable or better Canon lens? Maybe with IS?
Steve C
Steve Cherry
The DailyFrame
The DailyFrame
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text:
I arrived home late at night and my wife began to throw objects at me and scream in my face, So I then called her a Crazy Ass Bitch and left.
by 386obc May 20, 2008
The vengeful act of crapping on a lover's chest while they sleep.Buy the plush
When you try to have a casual conversation with a woman, and she threatens to phone the cops on you for harassment.
"I tried talking to Birgit about helping her daughter and that crazy ass bitch phoned the cops on me with her cell phone at the community center."
by ThisIsMe01xoxo June 06, 2012


text: I was nervous because I needed Kerley and my Kicker Matt Bryant to get me a combined 10 pts to win the matchup for the week. Like halfway through the second I got really nervous when they had like a combined 2 pts, I didn't think that they were going to be able to get me enough pts and then Kerley gets the TD haha. Kaep is killing me though 9pts... I am 3-2 but I mean I should be 4-1, if Kaep came to play I would have pulled out another win.


text:
SEE Turtles protects endangered sea turtles through unique conservation & volunteer trips, education, and Our Billion Baby Turtles initiative
Unique opportunities to participate in wildlife conservation programs around Latin America. Check out our hands-on tours to Costa Rica, Cuba, Mexico, and more.
Helping students learn about and experience turtle conservation. Free lesson plans, field trips, classroom presentations, and fundraisers for conservation.
Six of seven sea turtle species around the world are endangered or threatened. For every dollar, we can save one turtle hatchling with our partners around the world.
Feature Sea Turtle Conservation Tours
Sea Turtle School Programs
Photo Credits: Neil Ever Osborne & Solvin Zankl/Wild Wonders of Europe (banner images), Elizabeth Moreno


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by Egnyte
Jun 18, 2013
As IT and users fight the data deluge brought on by big data, social networks and multimedia, the benefits of implementing enterprise-class file sharing quickly come to light.
Almost every business has had to deal with mailbox bloat: attachments ranging from presentations to videos that end up in the inboxes and outboxes of email systems. Beyond clogging mail server arteries, the constant email barrage can leave collaborating teams wondering which versions of what document have the latest changes. Many organizations have turned to free file sharing services, only to discover that their lack of security, authentication and central control can introduce new levels of risk that far outweigh the reward. Enterprise-class file sharing solutions need to offer simple authentication of authorized users, ideally based on existing enterprise directories.
Fortunately, a "best-of-all-worlds" solution exists to bring all constituents into the corporate fold while offering the best possible performance in every environment. A hybrid on-premises and cloud approach to file sharing and synchronization unlocks new capabilities not possible until now, including uninterrupted online and offline access, integrated mobile workflows and a global view of all shared files regardless of where data resides.


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World's Most Dangerous Road and Potosi
Trip Start Jul 31, 2005
118Trip End Feb 18, 2007
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A climb of around a kilometre from La Paz, and almost 5km above sea level, is the start of the world's most dangerous road. It's a road which plunges some 3500 metres as it snakes it's way down from the Andes to the edge of the Amazon basin. It's known as the world's most dangerous road because it has the highest fatalities per usage anywhere. One look at the road and it's no wonder why this is the case. Most of the road is just a dirt track, two to three metres wide, with a 500 metre vertical drop to your left hand side and no crash barriers. Buses and lorries hardly fit on the road, so several go over the side every year, contributing to an annual death toll of between 200-300 people, which normally includes a few foreign tourists on Mountain Bikes.
So, of course, the best way to travel down this road is to put your life in your own hands, and not somebody else's, and get on bicycle
Early that morning, we met our group and our guides, and loaded our equipment on to the minibus. After an hour's climb up to 4700 metres, we unloaded the van at the point where the road starts to descend. After getting a safety briefing from the guides and getting our brakes checked, we set off on our way. The first hour or so of the trip is great, although at this altitude it's a little cold. You whisk past the tops of the snow capped Andes at exhilaratingly fast speeds, helped by a gradual descent and a proper paved road. I was clocking up speeds so fast, that I was actually easily overtaking buses and trucks as I descended. However, after around an hour of cycling the nice road stops, and you transfer to a road which is little more than a dirt track, and the start of the world's most dangerous road.
Just as we reached the start of the most dangerous section, a tropical storm started. The world's most dangerous road had now turned into the world's most dangerous river
The only benefit of the thick driving rain was that it partially obscured the reality of the drop from us, but one thing is for certain, one mistake on this road and you're a goner. We passed many a hairpin bend, where head on collisions have caused the lighter vehicle to be catapulted off the road and off the cliff
To our relief, everybody in the group survived the most dangerous section of the road, and as we left it behind, the rain stopped and the sun came out, perfect timing not. We had already come down far enough to have reached semi-tropical jungle, and the temperature had consequently risen substantially. As we continued down for the last hour of our trip, the road had turned extremely dusty, and any passing vehicle left a huge cloud of dust, obscuring our view for a couple of minutes. This poor visibility caused one girl on our trip to hit a rock in the road, come off her bike and break an arm. As we reached the bottom, we were greeted by the lead guide and sat down for a well earned beer. The guide then told us that the storm today caused the worst conditions he's seen for 5 years. It also meant that the trip photographer was unable to take photos for a lot of the time, so I had to borrow some of the Travelpod shots from friends who did the same tour a couple of days later. The conditions and the couple of close shaves which I had myself meant that although I thought the ride was exhilarating, once is enough
If this has interested you, I've found a BBC article on the road which goes into even more detail:- The world's most dangerous road
The Flying Potato Market
Patty had walked down to the travel agency to pick up an extremely muddy Marc. As we walked back to our hotel, we passed a quaint market selling dozens of varieties of potatoes. What we didn't know is that the market has a special tourist attraction. As you take your camera out to take a photo, the indigenous ladies start to throw potatoes at you. One hit Patty, and the other one just missed the camera, so we stormed over to them in a temper.
Us: "What the fuck do you think you're doing throwing potatoes at us?"
Indigenous Lady: "You're taking a photo of me and I don't like it!"
Patty: "I'm taking a photo of the street not of you, the street's not your personal property is it?"
Indigenous Lady: "Well, we don't like people even taking photos of the street"
Us: "Well that's not a reason to throw potatoes at people and if you ever throw a potato at us again, we'll pick up the whole sack and dump it over your head!"
I know this response sounds a bit harsh, but she threw the potatoes at us with such force she was obviously intending to hurt us, so it really wound us up
Traveling Around Bolivia
Taking coaches in the day in Bolivia are bad enough, so there's absolutely no way you'd want to spend the night on one. Bumpy roads, sod all leg room, noisy engines and disgusting smells all combine to ensure you wouldn't get one wink of sleep. So imagine our delight when we were told by every travel agency we entered in La Paz that the only way to our next destination Potosi, is on a night bus. If this had been Europe, we probably would have believed the answers we were getting, but with us now being well experienced Latin American travellers, we know very well that customer service related people here tend to talk through their ass. So out comes the map, and we decide to risk a three hour bus trip to the town of Osorno, which is on the way to Potosi and try our luck from there.
Potosi, the Highest City in the World
Just as well we're stubborn travellers, as from Osorno there were almost hourly buses to Potosi, mmmm thought there was no way to get there in the day. Anyway, 6 hours after we left Osorno, we arrive in Potosi
The main thing to do in Potosi is a mine tour. Unfortunately, both Patty and I have fallen ill with almost unstoppable Diarrhea, so rather than checking out the tourist sights in and around Potosi, we've checked in to the best hotel in town and are spending the time resting, trying to shake off the bug. We eventually shifted the bug with the help of some antibiotics. Before leaving Potosi, we storm into the restaurant which gave us the food poisoning and ask to speak to the manager. It was quite amusing, as the manager came out to the centre of the restaurant to speak to us, and as we were explaining our case, the customers could hear everything that was being said. As we turned around to leave the restaurant, we realised that everybody had stopped eating, mmmmm we wonder why:-)
Onward to Uyuni
From Potosi we took a 5 hour day bus to Uyuni
On the way there, we saw another reason for avoiding night buses in Bolivia. The previous night's bus to Uyuni had crashed with a car on a blind corner and both vehicles were still sprawled over the road. The bus, being the bigger of the two had not come off too badly, and hopefully the passengers would have escaped with just cuts and bruises, but there's no way that anybody could have survived from the car. If the bus had hit another bus or a lorry then we could have been looking at a large loss of life. It was really sad to see, but some passengers from our bus were lifting up bits of the car wreckage, looking for anything they could find worth taking.
We arrive in Uyuni, and as soon as we step off the bus, Patricia recognised a Dutch guy from our tour in Tasmania, Australia. We're used to bumping into people we've met before on the typical Gringo trail down from Ecuador, but a chance meeting like this with somebody that we last saw so far away seemed extra weird.
Finally, I think this entry will really test if my mum actually reads my Travelpod.


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It's Shopping Saturday! As we salute our American heroes this Memorial Day weekend, our ever-popular freebie free-for-all goes coupon crazy so you can save at the big holiday sales. Our list is packed with retail coupons, freebies, dining deals and fun things to do. Use it to save right through Monday.
"Like" our Sentinel Deals page on Facebook; follow Doreen Christensen on Twitter@PrettyGoodIdeas and sign up for Deals text alerts.
Coupons and retail deals
10 percent off for veterans and active-duty at Home Depot and Lowe's through Monday
20 percent off clearance at Bloomingdale's; expires Moday
$20 off $45 purchase at Yankee Candle; expires June 2
20 percent off one item at Toys R Us; expires Saturday
$30 off $100 purchase at Casual Male; expires Monday
15 percent off at Kohl's; expires
40 percent off one item at Michael's; expires Saturday
$10 OFF $30 purchase on men's at Kohl's; expires Saturday
$10 off $30 purchase at Teavana; expires June 2
$5 off $25 purchase at Dollar General; expires Saturday
$10 off $20 purchase at GNC; expires May 31
40 percent off clearance at Stein Mart; expires May 27
10 percent off entire purchase at Old Navy; expires June 5
Free canvas gloves with $20 purchase at Ace Hardware; through Facebook; expires May 31
Publix launches new Coupon Saver Tool matching sales to coupons
Sign up and save with mobile coupons from Macy's, Target, Bed, Bath & Bedyond and more
15 percent off at Sports Authority; expires Monday
$5 off at Home Depot via email
20 percent off at Ulta Beauty; expires June 1
$10 off with $30 purchase at Radio Shack; expires June 1
$5 off oil change at Jiffy Lube; expires January 2014
Free 60-day membership at BJ's Wholesale Club; expires July 14
$5 off $50 purchase from Home Depot with email signup
$5 off at SuperCuts with mobile offer
Couponing 101: How I save $450 on my grocery bill
Couponing 101: How to do a "moneymaker"
Target grocery coupons (accepted at many Publix Markets)
Grocery coupons from Coupons.com
Grocery coupons from SmartSource.com
Whole Foods Market coupons (accepted at many Publix Markets)
Staples coupons (print or show on your smartphone)
Free Tipsy Tows from AAA through Monday
Free access to military records on Ancestry.com through Monday
Medium Slurpees for 49 cents at 7-Eleven
Free entree at Pei Wei with gift card purchase; expires May 26
Save 30 percent at Miami Seaquarium for Miami Heat fans
Free sample of Garnier BB Cream; through Facebook
Free pastry or sweet treat at Panera Bread
free $10 gift card and free shipping from L'Occitane; expires May 30
Free Redbox movie rental
Free bowling for kids through September
rFee brake check or tire rotation valued at $15 at Sears Auto Centers; expires June 1
Free bottle of Biotrue Contact Solution valued at $3.99 from Bausch+Lomb
Free $25 blowout with purchase of another for Mom at SoBlo Blowdry Salon; expires May 31
Publix launches new Coupon Saver Tool matching sales to coupons
Save $3 off admission to Fort Lauderdale Home and Remodeling Show Saturday-Monday
$10 off at Buca di Beppo; expires May 27
Retail news: Walmart Neighborhood Market opening in Deerfield Beach
10 percent with new Staples teacher rewards program
Free mini Matrix Biolage shampoo and conditioner with service at JC Penney Salon
Win $10,000 and other prizes with 50 billionth Apple App download
Coupon: $1 McDonald's Egg White Delight; expires June 20
Free "Iron Man 3" tickets with pizza purchase
Free Publix Shopping Spree book with $40 in coupons
Free ticket with purchase of another to see "The Big Wedding"
Free haircuts for unemployed workers at Salon 44 in Lauderhill; expires Juy 31
Get Shop-O-Matic deals and bargains sent right to your inbox and phone
Free and reduced-priced prescriptions at South Florida pharmacies
Free samples from P&G Everyday; expires June 1
Free Smartphone with 2-year agreement from CVS/Pharmacy
Save 15 cents a gallon on gas from Walmart
Free Stuffed Pizza Rollers from Pizza Hut with email sign-up
Free 60-day membership at BJ's Wholesale Club; expires July 14
Free health tests and AARP membership from Walgreens; expires June 30
Digital coupons now online in Publix stores
Free health screenings at Sam's Club on Saturdays each month
Free 25 4X6 photos from Walmart Photo Center
Free samples and high-value coupons from VocalPoint.com
Free appetizer valued at $8 with free app download from T.G.I. Friday's
Trade unused gift cards for credit at CVS/Pharmacy
Free Physicians Formula cosmetics with rebates valued at up to $25
Free Blizzard treat from Dairy Queen with Fan Cub signup
Free lens cloth and cleaner from Walmart Vision Center
Free beauty gifts on your birthday
Free $129 annual pass for Florida teachers at Legoland Florida; expires Dec. 31
Free month of Redbox Instant Streaming Video ($8 value)
Free bowling valued at up to $6 from Musselman's; expires Aug. 31
Dining Deals
PDQ: Buy one, get one free platter of 25 or 50 tenders on Monday
Flanigans: $10 off $20 purchase; expires Wednesday
Hooters: 10 free wings for military on Memorial Day
Buca di Beppo: $10 off $20 purchase; expires May 27
Brio Tuscan Grille: $10 of two lunch entrees or $15 off two dinners; expires May 31
Waffle House: Free hashbrowns Monday-Friday; expires June 3
Dunkin Donuts: $1 off dozen and $1 off breakfast sandwich (mobile coupons)
IHOP: Three free meals valued at $7.99 each with e-club sign-up.
Pizza Hut Free Stuffed Pizza Rollers from with email sign up
Hooters $6.99 for 10 wings and fries at on Wednesdays
IKEA Free eats on Mondays and Tuesday
Pizza Hut Free Stuffed Pizza Rollers
Things to do
50 percent off South Florida theater tickets from CulturalConnection.org
Free Build and Grow Kids Clinic at Lowe's at 10 a.m. Saturday
Free workshops at The Home Depot on Saturdays and Sundays
Free guitar classes on Saturdays at Guitar Centers
Free Technique Cooking Classes at Williams-Sonoma in April


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SPECIAL OFFER! Free dynamic mic worth £79.00 with all Sontronic mics...
To celebrate the 5th anniversary of Sontronics, anyone in the UK or Ireland purchasing a new Sontronics microphone from Dolphin Music between 14th January and the 28th of February will be able to claim a free STC-80 Dynamic Mic worth £79.00!
The Sontronics brand was launched at the NAMM show in 2005 and their products are all designed and developed in the UK. Included in the range are studio condensers, valve mics, ribbon mics and handhelds as well as mic capsules, stands, cables, popshields and the 100% British-designed, European-made Chimera and Sonora pre-amplifiers. The most recent addition to the Sontronics catalogue was the Delta ribbon microphone which recently received a Future Music Platinum Award.
To claim their free STC-80, the customer simply needs to complete the online rebate form at http://www.timespace.com/sontronics, send it to T+S with proof of purchase and their free microphone will be shipped to them via courier at no cost.
*Promotion includes the following microphones; STC-1, STC-1S, STC-2, STC-6, Orpheus, Helios, Omega, Sigma, Delta. It does not include the STC-80 and is subject to terms and conditions.
Related Products
Sontronics STC-6 Handheld condenser microphone
Sontronics STC-6 The Sontronics STC-6 builds upon the success of its predecessor, the STC-5, with an innovative new design and pro level features.The mic features a studio-grade, gold-sputtered cardioid capsule to ensure cystal clear clarity and a powerful performance time after time. Being more sensitive than a dynamic microphone, the STC-6 captures your voice in significantly more detail,…
Web Price:129.00
Availability:Normally 7-10 Days
Sontronics Delta Ribbon Microphone
Following on from the worldwide success of our iconic SIGMA ribbon microphone, Sontronics have introduced the DELTA. Where SIGMA found its place in the heart of the studio and recording world, DELTA's incredible capability in miking guitar cabinets sets it up to become a new standard in live sound recording. …
Web Price:438.99
Availability:Normally 7-10 Days


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Another new beekeeper here with lots of questions. Started the year out with two hives. One of them suffered from lack of a queen, layings workers, severe robbing and finally failed. The other seems to be going gangbusters. Two deeps with lots of honey, one medium super fill to the brim, and another medium super that the bees are currently working on. The goldenrod flow, in my opinion, is very strong and still going on. I started a treatment program the middle of August including the insertion of Check-mite II. The strips will be coming out on the 24th of this month. Most, if not all, of the honey in the medium supers was stored while the strips have been in, so, not appropriate for human consumption. Should I:
1. Just leave everything as is? Don't remove the supers assuring a good supply of honey for the winter?
2. Remove the mediums and extract? Save the honey for feeding later on in the winter or spring. Let the bees clean up the frames of residue honey? If so....how?
3. Remove the mediums and place in a freezer to be re-applied to the hive when needed or even use to make nucs?
4. I am open to suggestions. Any and all will be appreciated.


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I just had a thought. In feral hives, bees build up their store of honey and pollen, and swarm, generally speaking. I'm not saying it's in that order or anything, just what they do. In the winter of course, they eat the honey and in the spring they use the pollen to build up again.
But what about long term honey storage? Suppose the cavity the bees are living in is a little large. They build up, store a lot of honey, more than they consume during any given winter. What is done with this long term honey? What do beekeepers do that interfere with the bees' honey storage characteristics? Few surviving hives use all their stores down to the last cell. There should be some left over in the spring and in a colony with certain characteristics, there might be a substantial amount.
So there's a couple of things that I see that interfere. First, we confiscate what we consider the 'surplus.' I doubt if a bee had an opinion, they would consider their hard earned bank account a 'surplus.'
Then there is a lot of feeding going on because for the most part, beekeepers don't take the 'surplus,' they take the honey, and the bees often then don't have enough to overwinter. Some beekeepers are more conscientious about this, yes, but there is a whole lot of feeding going on.
Enter another aspect of beekeeping, changing the hive size, or as it's known more colloquially, 'supering.' Like migration to almonds, this doesn't happen in the wild. This almost certainly affects hive dynamics, and we see examples of it all the time. Sometimes bees won't 'move up.' They swarm without the hive being full. And you gotta worry about wax moths getting into the stored comb.
All these things work against a natural longer term storage of honey, honey that might be available in a drought year, or an extended cold wet spring, or an especially harsh winter. But there are also beekeepers who by practice simply don't feed, expecting the bees to compensate for the above actions on the part of the beekeeper.
I suggest a more conscientious approach to beekeeping. I suggest leaving comb on the hive year 'round, leaving enough honey (plus a factor of safety) for the bees to survive the winter unfed, and very limited supplementation only when necessary to prevent starvation of colonies which through the sole responsibility of the beekeeper (or perhaps of abnormal weather) do not have enough stores to last the winter. I also would like to get away from the idea of 'feed.' It is nectar substitute just like pollen substitute. And there's nothing like the real thing. Bees ought to collect nectar and pollen on their own, it's what they do.


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Sam Berns died last week, at the age of 17.
I never knew him, but he touched my heart - and those of so many others.
I first saw his picture years ago. A teenager weighing 50 pounds and looking like a man in his 70s, facing almost certain death sooner rather than later, is not someone you easily forget. Sam had a rare disease known as progeria. He was diagnosed at 22 months. The average life expectancy for children with this disease is 13 years. Sam beat the odds, by four years, but that isn't what made him special.
When he was 13, he agreed to be followed (as it turned out, for the next three years) by Oscar-winning documentarians Sean Fine and Andrea Nix Fine. There was only one condition, which he made clear at the outset: "I didn't put myself in front of you to have you feel bad for me," he says. "You don't need to feel bad for me. Because I want you to get to know me. This is my life."
I did feel bad for him, very bad, for him and for his parents and family. But that's my problem, not his. What is remarkable is that he didn't seem to feel sorry for himself.
He lived his life with gusto. He was an Eagle Scout and a huge sports fan who loved math and science and was passionate about drumming. A high school junior, he was planning to apply to college when he died.
Sam is not the only hero of this story.
Both of his parents are pediatricians. He was their only child. It is hard to imagine just how devastating it must have been for his parents, whose work is to heal other children, to learn that their precious son suffered from a rare disease for which there is no cure.
At the time of his diagnosis, there was no foundation or institute studying this disease. If you're going to get sick, one of my friends said to me years ago, best to get something that a lot of other people (preferably including some celebrities and gazillionaires) also have. Progeria is a rare disease. There were no celebrities pumping money in to find a cure.
Sam's parents aren't celebrities, and they aren't gazillionaires, but they have medical degrees and an amazing family. In 1999, the year after Sam's diagnosis, they founded the Progeria Research Foundation, based in Peabody, Mass., north of Boston, two towns away from where I grew up. The executive director is Sam's aunt. Another aunt runs the website. The medical director is his mother.
A team that included his mother found the gene that causes progeria. Another team found the first treatment, which began clinical trial in 2007. The most recent clinical trial began in 2012. There is still no cure.
In a TEDx talk, Sam shared his wish: to march with his high school band playing the snare drum. But he couldn't, because he weighed 50 pounds and the drum and harness weighed 40 pounds. His parents, happily, had the resources to find an engineer to make a 6-pound harness. Sam got his wish.
The website includes videos from other children with this terrible disease. In hers, Ashley speaks to other children, telling them not to get upset when people stare, because they may not know what progeria is. When her chest hurts, she says, she tries to focus on other things.
Sam wanted to change the world. "No matter what I choose to become, I believe that I can change the world. And as I'm striving to change the world, I will be happy."
He did change the world. Someday, thanks in no small part to Sam and his family, there will be a cure. But even more, he will live on as an inspiration to anyone who watches the documentary or reads his words or just sees his picture. If Sam Berns could be happy, with all that he faced, then perhaps the rest of us can hold on to his spirit and find happiness in our own lives.
May he rest in peace.
Check out these recently discussed stories and voice your opinion...


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First Look: 2012 Aston Martin VirageJust Like the Ford Days: A New Virage Returns to the FrayIt will take more than 200 man-hours to build just one car, but we'd expect nothing less from the esteemed Gaydon, Warwickshire-based Aston Martin company. After 15 years, the Virage is coming back to the United States, and it looks decidedly more modern this time around.In its day, the original Virage was heralded as the next great Aston, a daring project that took a bold step away from the V-8s of the time. Today, there's little pressure on the new model. It will stand on its own, slotted between the DB9 and DBS, although this time around, you'll have a hard time distinguishing it from its brethren.
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I hope Lincoln gets this brand's engine lineup. When does the contract run out between Ford and Aston Martin?
I assume this is the coupe version of the Rapide. Very sexy though.
_______________Your choices are white and of course black___________________
I love Aston Martins, but did they really need a car to slot in between the DB9 and DBS? Think about it, they have the DBS (V12 powered 2-door coupe), DB9 (V12 powered V12 coupe), and V12 Vantage (V12 powered 2-door coupe). Do they really need a fourth V12 powered 2-door coupe? I think the resources would have been better spent developing the next generation chassis.
^^^ good point but hey it looks sweet and if I win powerball, (guess you gotta play to win) id buy one!
DBS...still the best and most beautiful Aston Martin.
Admittedly, I'm not the most knowledgeable on Aston's lineup, but I don't see the point either. I'm assuming this is based on an existing model, the DB9 or DBS? I dunno.
____________________Because it totally worked when Lincoln did it.


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Norwich have confirmed the signing of midfielder Jonas Gutierrez on loan from Newcastle for the rest of the season.
The 30-year-old effectively took his leave of the Magpies over the weekend when he posted a series of farewell messages on his personal Twitter account suggesting that his time at the club was over.
Gutierrez will link-up once again with Norwich manager Chris Hughton, who was in charge at St James' Park between June 2009 and December 2010, as he led the Magpies out of the Championship and back into the top flight.
Norwich are certainly in need of reinforcements as they look to pull clear of the relegation zone, with the Canaries in 15th place but only two points ahead of 18th-placed Cardiff.
Hughton feels Gutierrez's Premier League experience can benefit his squad in the fight to secure top-flight survival.
He said on the club's official website, http://www.canaries.co.uk, following confirmation of the move: "Jonas is somebody that will certainly bring experience - he has played close to 200 games for Newcastle, so he knows the Premier League very well.
"He has been in England for five years, so there won't be that settling in period that you would have with some other players, and that is important, particularly in January when you need players that can go straight into the squad.
"Jonas can play on either flank and in a central position, so he's a very welcome addition and we look forward to working with him."
Argentina international Gutierrez joined Newcastle from Real Mallorca during the summer of 2008, when he signed a five-year contract.
He has made 195 appearances for the club and scored 11 goals, although has figured only twice this season, starting the 4-0 defeat by Manchester City on the opening weekend of the campaign and then coming on as a substitute in the 2-1 Premier League victory at Cardiff on October 5.
Gutierrez hopes he can make an instant impact at Carrow Road.
"It is an opportunity for me to get back in the game and to try and do my best for the team," he said on http://www.canaries.co.uk.
"Personally I want to do the right things on the pitch and win my place, and then for the team we want to finish as high as we can.
"It is a tough league, all the games are difficult, but we have a good opportunity."
Norwich are in action on Tuesday night with a trip to Craven Cottage for their FA Cup third-round replay against Fulham.
The Canaries have no fresh injury problems ahead of the match, for which Hughton confirmed he would again utilise his squad as they look to secure a live fourth-round tie away to Sheffield United.
Hughton said at a press conference: "I am very keen to use the squad. We felt we should have finished the (first) game off at Carrow Road.
"We know what awaits us in the next round and that would give us that little lift, irrespective of the competition.
"Firstly we have to get through and we found to our detriment last season (against Luton) it is not always the fancied team who go through.
"I wouldn't see an away tie at Sheffield United as anything but a difficult game, so we need to make sure we put ourselves in a position to get through.
"The only thing we don't know is what team Fulham put out because they obviously made quite a few changes from the previous league game (for the first tie)."
Norwich's 18-year-old winger Josh Murphy could be handed another chance to impress, having started the first tie and was replaced by his twin brother Jacob late in the second half.
Hughton said: "He is certainly in the squad and I thought he was excellent in the first game. He is a young lad and maturing well.
"Fulham would have done their research for the first time, but they will definitely know him a little bit better now."
Despite the focus on getting through to the fourth round, Hughton accepts Norwich's priority must always be top-flight survival.
"The morale here is still good, but we are very conscious of how competitive the Premier League is," said Hughton, whose side have not won for six league games following the 2-0 defeat at Everton.
"We are a point behind Swansea, who have had really good periods this season.
"We know it is closing up (at the bottom of the table) and the only way to get away from that is to win games."
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A friend who has my ex-bees from 5 years ago, wanted to move the hive to someone else's house in town.
WHat's the concensus about how far you have to move the colony to disrupt their desire to return to the same old location? We think the new home is only 1/4 mile away, way too close.
He's thinking of moving them elsewhere for a day (basically leaving them in the pickup truck parked in the shade a few miles away).. I think a day isn't long enough for them to lose their 'homing' recollection of their old surroundings.
Does anyone know what the minimum time is to 'take them elsewhere' in order to ultimately move them within the same neighborhood?


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Authentic industry information through surveys, statistics, reports, studies as well information on the tourism ministry's plans, schemes, guidance notes, tenders, etc, in addition to a space to interact with your peers
Safety and Security of Tourist should be of Utmost Concern says Sahai
Safety and Security of tourist should be of utmost concern to everyone in the country. All stake holders including Centre, State Governments and other agencies should be fully involved in this task. This was stated by Union Minister for Tourism, Shri Subodh Kant Sahai while addressing a meeting in the Consultative Committee meeting attached to his Ministry, here today. Expressing concern over the recent abduction of foreign tourists in Odisha, the Minister said such incidents cause an adverse impact on the flow of foreign tourists to the country. Shri Sahai also called for investment friendly industrial policy for tourism sector in the country.