Wikimedia Commons has media related to Geobiography of Venkatraman Ramakrishnan .
Venkatraman "Venki" Ramakrishnan (born 1952)  is an American and British structural biologist of Indian origin. In 2009 he shared the Nobel Prize in Chemistry with Thomas A. Steitz and Ada Yonath, "for studies of the structure and function of the ribosome".     . He was elected President of the Royal Society for a term of five years starting in 2015.  .
Structural biology is a branch of molecular biology, biochemistry, and biophysics concerned with the molecular structure of biological macromolecules, how they acquire the structures they have, and how alterations in their structures affect their function. This subject is of great interest to biologists because macromolecules carry out most of the functions of cells, and it is only by coiling into specific three-dimensional shapes that they are able to perform these functions. This architecture, the "tertiary structure" of molecules, depends in a complicated way on each molecule's basic composition, or "primary structure."
Thomas Arthur Steitz was an American biochemist, a Sterling Professor of Molecular Biophysics and Biochemistry at Yale University, and investigator at the Howard Hughes Medical Institute, best known for his pioneering work on the ribosome.
The Cambridge Biomedical Campus is the largest centre of medical research and health science in Europe. Located at the southern end of Hills Road in Cambridge, England the campus is managed by the University of Cambridge. The site is funded by organisations such as the Cambridge University Hospitals NHS Foundation Trust, the Wellcome Trust, Cancer Research UK, the UK government's Medical Research Council and has National Institute for Health Research Biomedical Research Centre status. It is an accredited UK academic health science centre and home to Addenbrooke's Hospital and the university's medical school.
Donald Olding Hebb FRS was a Canadian psychologist who was influential in the area of neuropsychology, where he sought to understand how the function of neurons contributed to psychological processes such as learning. He is best known for his theory of Hebbian learning, which he introduced in his classic 1949 work The Organization of Behavior. He has been described as the father of neuropsychology and neural networks. A Review of General Psychology survey, published in 2002, ranked Hebb as the 19th most cited psychologist of the 20th century. His views on learning described behavior and thought in terms of brain function, explaining cognitive processes in terms of connections between neuron assemblies.
Vadodara is the third-largest city in the Indian state of Gujarat, after Ahmedabad and Surat. It is the administrative headquarters of Vadodara District and is located on the banks of the Vishwamitri river, 141 kilometres (88 mi) from the state capital Gandhinagar. The railway line and NH 8 that connect Delhi and Mumbai pass through Vadodara. It is known as a Sanskari city of India.
Ferroelectricity is a characteristic of certain materials that have a spontaneous electric polarization that can be reversed by the application of an external electric field. All ferroelectrics are pyroelectric, with the additional property that their natural electrical polarization is reversible. The term is used in analogy to ferromagnetism, in which a material exhibits a permanent magnetic moment. Ferromagnetism was already known when ferroelectricity was discovered in 1920 in Rochelle salt by Valasek. Thus, the prefix ferro, meaning iron, was used to describe the property despite the fact that most ferroelectric materials do not contain iron. Materials that are both ferroelectric and ferromagnetic are known as multiferroics.
He continued to work on ribosomes from 1983-95 as a staff scientist at Brookhaven National Laboratory.  In 1995 he moved to the University of Utah as a Professor of Biochemistry, and in 1999, he moved to his current position at the Medical Research Council Laboratory of Molecular Biology in Cambridge, England, where he had also been a sabbatical visitor during 1991-92 on a Guggenheim Fellowship.
In 1999, Ramakrishnan's laboratory published a 5.5 Angstrom resolution structure of the 30S subunit. The following year, his laboratory determined the complete molecular structure of the 30S subunit of the ribosome and its complexes with several antibiotics. This was followed by studies that provided structural insights into the mechanism that ensures the fidelity of protein biosynthesis. In 2007, his laboratory determined the atomic structure of the whole ribosome in complex with its tRNA and mRNA ligands. Since 2013, he has primarily used cryo-EM to determine new ribosome structures.   Ramakrishnan is also known for his past work on histone and chromatin structure.
The ribosome is a complex molecular machine, found within all living cells, that serves as the site of biological protein synthesis (translation). Ribosomes link amino acids together in the order specified by messenger RNA (mRNA) molecules. Ribosomes consist of two major components: the small ribosomal subunits, which read the RNA, and the large subunits, which join amino acids to form a polypeptide chain. Each subunit consists of one or more ribosomal RNA (rRNA) molecules and a variety of ribosomal proteins. The ribosomes and associated molecules are also known as the translational apparatus.
Prokaryotic translation is the process by which messenger RNA is translated into proteins in prokaryotes.
Eukaryotic translation is the biological process by which messenger RNA is translated into proteins in eukaryotes. It consists of four phases: initiation, elongation, termination, and recycling.
A ribosomal protein is any of the proteins that, in conjunction with rRNA, make up the ribosomal subunits involved in the cellular process of translation. A large part of the knowledge about these organic molecules has come from the study of E. coli ribosomes. All ribosomal proteins have been isolated and many specific antibodies have been produced. These, together with electronic microscopy and the use of certain reactives, have allowed for the determination of the topography of the proteins in the ribosome. E. coli, other bacteria and Archaea have a 30S small subunit and a 50S large subunit, whereas humans and yeasts have a 40S small subunit and a 60S large subunit. Equivalent subunits are frequently numbered differently between bacteria, Archaea, yeasts and humans. More recently, a near-complete (near)atomic picture of the ribosomal proteins is emerging from the latest high-resolution cryo-EM data.
Eukaryotic initiation factors (eIFs) are proteins or protein complexes involved in the initiation phase of eukaryotic translation. These proteins help stabilize the formation of ribosomal preinitiation complexes around the start codon and are an important input for post-transcription gene regulation. Several initiation factors form a complex with the small 40S ribosomal subunit and Met-tRNAiMet called the 43S preinitiation complex. Additional factors of the eIF4F complex recruit the 43S PIC to the five-prime cap structure of the mRNA, from which the 43S particle scans 5'-->3' along the mRNA to reach an AUG start codon. Recognition of the start codon by the Met-tRNAiMet promotes gated phosphate and eIF1 release to form the 48S preinitiation complex, followed by large 60S ribosomal subunit recruitment to form the 80S ribosome. There exist many more eukaryotic initiation factors than prokaryotic initiation factors, reflecting the greater biological complexity of eukaryotic translation. There are at least twelve eukaryotic initiation factors, composed of many more polypeptides, and these are described below.
The 5S ribosomal RNA is an approximately 120 nucleotide-long ribosomal RNA molecule with a mass of 40 kDa. It is a structural and functional component of the large subunit of the ribosome in all domains of life, with the exception of mitochondrial ribosomes of fungi and animals. The designation 5S refers to the molecule's sedimentation velocity in an ultracentrifuge, which is measured in Svedberg units (S).
The prokaryotic small ribosomal subunit, or 30S subunit, is the smaller subunit of the 70S ribosome found in prokaryotes. It is a complex of the 16S ribosomal RNA (rRNA) and 19 proteins. This complex is implicated in the binding of transfer RNA to messenger RNA (mRNA). The small subunit is responsible for the binding and the reading of the mRNA during translation. The small subunit, both the rRNA and its proteins, complexes with the large 50S subunit to form the 70S prokaryotic ribosome in prokaryotic cells. This 70S ribosome is then used to translate mRNA into proteins.
Ribosomal particles are denoted according to their sedimentation coefficients in Svedberg units. The 60S subunit is the large subunit of eukaryotic 80S ribosomes. It is structurally and functionally related to the 50S subunit of 70S prokaryotic ribosomes. However, the 60S subunit is much larger than the prokaryotic 50S subunit and contains many additional protein segments, as well as ribosomal RNA expansion segments.
EF-G is a prokaryotic elongation factor involved in protein translation. As a GTPase, EF-G catalyzes the movement (translocation) of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome.
The eukaryotic small ribosomal subunit (40S) is the smaller subunit of the eukaryotic 80S ribosomes, with the other major component being the large ribosomal subunit (60S). The "40S" and "60S" names originate from the convention that ribosomal particles are denoted according to their sedimentation coefficients in Svedberg units. It is structurally and functionally related to the 30S subunit of 70S prokaryotic ribosomes. However, the 40S subunit is much larger than the prokaryotic 30S subunit and contains many additional protein segments, as well as rRNA expansion segments.
Ribosomes are a large and complex molecular machine that catalyzes the synthesis of proteins, referred to as translation. The ribosome selects aminoacylated transfer RNAs (tRNAs) based on the sequence of a protein-encoding messenger RNA (mRNA) and covalently links the amino acids into a polypeptide chain. Ribosomes from all organisms share a highly conserved catalytic center. However, the ribosomes of eukaryotes are much larger than prokaryotic ribosomes and subject to more complex regulation and biogenesis pathways. Eukaryotic ribosomes are also known as 80S ribosomes, referring to their sedimentation coefficients in Svedberg units, because they sediment faster than the prokaryotic (70S) ribosomes. Eukaryotic ribosomes have two unequal subunits, designated small subunit (40S) and large subunit (60S) according to their sedimentation coefficients. Both subunits contain dozens of ribosomal proteins arranged on a scaffold composed of ribosomal RNA (rRNA). The small subunit monitors the complementarity between tRNA anticodon and mRNA, while the large subunit catalyzes peptide bond formation.
Translational regulation refers to the control of the levels of protein synthesized from its mRNA. This regulation is vastly important to the cellular response to stressors, growth cues, and differentiation. In comparison to transcriptional regulation, it results in much more immediate cellular adjustment through direct regulation of protein concentration. The corresponding mechanisms are primarily targeted on the control of ribosome recruitment on the initiation codon, but can also involve modulation of peptide elongation, termination of protein synthesis, or ribosome biogenesis. While these general concepts are widely conserved, some of the finer details in this sort of regulation have been proven to differ between prokaryotic and eukaryotic organisms.
The term macromolecular assembly (MA) refers to massive chemical structures such as viruses and non-biologic nanoparticles, cellular organelles and membranes and ribosomes, etc. that are complex mixtures of polypeptide, polynucleotide, polysaccharide or other polymeric macromolecules. They are generally of more than one of these types, and the mixtures are defined spatially, and with regard to their underlying chemical composition and structure. Macromolecules are found in living and nonliving things, and are composed of many hundreds or thousands of atoms held together by covalent bonds; they are often characterized by repeating units. Assemblies of these can likewise be biologic or non-biologic, though the MA term is more commonly applied in biology, and the term supramolecular assembly is more often applied in non-biologic contexts. MAs of macromolecules are held in their defined forms by non-covalent intermolecular interactions, and can be in either non-repeating structures, or in repeating linear, circular, spiral, or other patterns. The process by which MAs are formed has been termed molecular self-assembly, a term especially applied in non-biologic contexts. A wide variety of physical/biophysical, chemical/biochemical, and computational methods exist for the study of MA; given the scale of MAs, efforts to elaborate their composition and structure and discern mechanisms underlying their functions are at the forefront of modern structure science.
In molecular biology, VAR1 protein domain, otherwise known as variant protein 1, is a ribosomal protein that forms part of the small ribosomal subunit in yeast mitochondria. Mitochondria possess their own ribosomes responsible for the synthesis of a small number of proteins encoded by the mitochondrial genome. VAR1 is the only protein in the yeast mitochondrial ribosome to be encoded in the mitochondria - the remaining approximately 80 ribosomal proteins are encoded in the nucleus. VAR1 along with 15S rRNA are necessary for the formation of mature 37S subunits.
Ada E. Yonath is an Israeli crystallographer best known for her pioneering work on the structure of the ribosome. She is the current director of the Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly of the Weizmann Institute of Science.
50S ribosomal protein L25 is a protein that in Escherichia coli is encoded by the rplY gene.
Andrew P. Carter is a British structural biologist who works at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) in Cambridge, UK. He is known for his work on the microtubule motor dynein.
1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 "Venkatraman Ramakrishnan - Biography: From Chidambaram to Cambridge: A Life in Science". nobelprize.org. Stockholm. Archived from the original on 2015-04-18.
1 2 "2009 Chemistry Nobel Laureates". Nobel Foundation. 2009. Retrieved 2009-10-14.
1 2 "No. 60009". The London Gazette (Supplement). 31 December 2011. p. 1.
1 2 Cerf, Corinne; Lippens, Guy; Muyldermans, Serge; Segers, Alain; Ramakrishnan, V.; Wodak, Shoshana J.; Hallenga, Klaas; Wyns, Lode (1993). "Homo- and heteronuclear two-dimensional NMR". Biochemistry. 32 (42): 11345–11351. doi:10.1021/bi00093a011.
1 2 Ramakrishnan, Venkatraman; Tanaka, Tomoyasu (1977). "Green's-function theory of the ferroelectric phase transition in potassium dihydrogen phosphate (KDP)". Physical Review B . 16 (1): 422–426. doi:10.1103/physrevb.16.422.
1 2 James, Nathan Rhys (2017). Structural insights into noncanonical mechanisms of translation. cam.ac.uk (PhD thesis). University of Cambridge. doi:10.17863/CAM.13713. OCLC 1064932062. EThOS uk.bl.ethos.725540.
↑ Rodnina, Marina V.; Wintermeyer, Wolfgang (2010). "The ribosome goes Nobel". Trends in Biochemical Sciences. 35 (1): 1–5. doi:10.1016/j.tibs.2009.11.003. PMID 19962317.
1 2 3 "Venkatraman_Ramakrishnan". University of Cambridge. Archived from the original on 2015-04-19.
↑ Peplow, M. (2015). "Structural biologist named president of UK Royal Society". Nature. doi:10.1038/nature.2015.17153.
↑ Nair, Prashant (2011). "Profile of Venkatraman Ramakrishnan". Proceedings of the National Academy of Sciences . 108 (38): 15676–15678. doi:10.1073/pnas.1113044108. PMC 3179092 . PMID 21914843.
↑ "Biologist Venki Ramakrishnan to lead Royal Society". London: BBC News. 2015-03-18. Archived from the original on 2015-10-10.
↑ Ramakrishnan, Venki (2018). Gene machine. The race to decipher the secrets of the ribosome. London: Oneworld. ISBN 9781786074362. OCLC 1080631601.
↑ "Common root: Tamil Nadu gets its third laureate". Times of India. TNN. 8 October 2009.
↑ Ramakrishnan, C. V.; Banerjee, B. N. (1951). "Mould Lipase: Effect of Addition of Vitamins and Sterol to the Cake Medium on the Growth and the Activity of the Lipolytic Mould". Nature. 168 (4282): 917–918. doi:10.1038/168917a0. PMID 14899529.
↑ Ramakrishnan, Rajalakshmi (1959). Comparative Effects of Successive and Simultaneous Presentation on Transfer in Verbal Learning (PhD thesis). McGill University.
↑ "Lalita Ramakrishnan Home page in Department of Medicine, University of Cambridge".
↑ "Lalita Ramakrishnan elected to the U.S. National Academy of Sciences". University of Cambridge. Retrieved 30 January 2016.
↑ Ramakrishnan, Venkatraman (1976). The Green function theory of the ferroelectric phase transition in KDP (PhD thesis). Ohio University. OCLC 3079828.
↑ "Venkatraman Ramakrishnan: a profile". Times of India. 2009-10-07. Retrieved 2009-10-07.
↑ "FACTBOX: Nobel chemistry prize – Who are the winners?". Reuters. 2009-10-07. Retrieved 2009-10-07.
↑ "Profile: Dr Venkatraman Ramakrishnan". Indian Express. 7 October 2009. Retrieved 2009-10-07.
↑ "Nobel laureate Venkat Ramakrishnan failed IIT, medical entrance tests". The Times Of India. 2010-01-05.
↑ Fernández, Israel S.; Bai, Xiao-Chen; Hussain, Tanweer; Kelley, Ann C.; Lorsch, Jon R.; Ramakrishnan, V.; Scheres, Sjors H. W. (2013-11-15). "Molecular architecture of a eukaryotic translational initiation complex". Science. 342 (6160): 1240585. doi:10.1126/science.1240585. ISSN 1095-9203. PMC 3836175 . PMID 24200810.
↑ Amunts, Alexey; Brown, Alan; Bai, Xiao-Chen; Llácer, Jose L.; Hussain, Tanweer; Emsley, Paul; Long, Fei; Murshudov, Garib; Scheres, Sjors H. W. (2014-03-28). "Structure of the yeast mitochondrial large ribosomal subunit". Science. 343 (6178): 1485–1489. doi:10.1126/science.1249410. ISSN 1095-9203. PMC 4046073 . PMID 24675956.
↑ Ramakrishnan, V.; Wimberly, Brian T.; Brodersen, Ditlev E.; Clemons, William M.; Morgan-Warren, Robert J.; Carter, Andrew P.; Vonrhein, Clemens; Hartsch, Thomas (2000). "Structure of the 30S ribosomal subunit". Nature . 407 (6802): 327–339. doi:10.1038/35030006. PMID 11014182.
↑ Ramakrishnan, V.; Carter, Andrew P.; Clemons, William M.; Brodersen, Ditlev E.; Morgan-Warren, Robert J.; Wimberly, Brian T. (2000). "Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics". Nature . 407 (6802): 340–348. doi:10.1038/35030019. PMID 11014183.
↑ Ramakrishnan, V.; Finch, J. T.; Graziano, V.; Lee, P. L.; Sweet, R. M. (1993). "Crystal structure of globular domain of histone H5 and its implications for nucleosome binding". Nature . 362 (6417): 219–223. doi:10.1038/362219a0. PMID 8384699.
↑ Ogle, J. M.; Brodersen, DE; Clemons, WM Jr; Tarry, MJ; Carter, AP; Ramakrishnan, V (2001). "Recognition of Cognate Transfer RNA by the 30S Ribosomal Subunit". Science . 292 (5518): 897–902. CiteSeerX 10.1.1.484.7460 . doi:10.1126/science.1060612. PMID 11340196.
↑ Semenza, C; Butterworth, B; Panzeri, M; Ferreri, T (1990). "Word formation: New evidence from aphasia". Neuropsychologia. 28 (5): 499–502. doi:10.1016/0028-3932(90)90075-y. PMID 1695997.
↑ Brodersen, Ditlev E.; Clemons, William M.; Carter, Andrew P.; Morgan-Warren, Robert J.; Wimberly, Brian T.; Ramakrishnan, V. (2000). "The Structural Basis for the Action of the Antibiotics Tetracycline, Pactamycin, and Hygromycin B on the 30S Ribosomal Subunit". Cell. 103 (7): 1143–1154. doi:10.1016/s0092-8674(00)00216-6. PMID 11163189.
↑ Ramakrishnan, V. (2002). "Ribosome Structure and the Mechanism of Translation". Cell. 108 (4): 557–572. doi:10.1016/s0092-8674(02)00619-0. PMID 11909526.
↑ Ogle, James M.; Murphy, Frank V.; Tarry, Michael J.; Ramakrishnan, V. (2002). "Selection of tRNA by the Ribosome Requires a Transition from an Open to a Closed Form". Cell. 111 (5): 721–732. doi:10.1016/s0092-8674(02)01086-3. PMID 12464183.
↑ Ian Tucke (15 July 2018). "Venkatraman Ramakrishnan: 'Britain's reputation has been hurt'". The Guardian.
↑ "The EMBO Pocket Directory" (PDF). European Molecular Biology Organization. Archived from the original (PDF) on 2015-03-16.
↑ "Sir Venki Ramakrishnan FRS". London: Royal Society. Archived from the original on 2015-09-06.
↑ "Emeritus and Honorary Fellows". Somerville College, Oxford . Retrieved 26 August 2018.
↑ "All Nobel Laureates in Chemistry". Nobel Foundation. Retrieved 2009-10-07.
↑ "Laureate - Venkatraman Ramakrishnan". Lindau Nobel Laureate Meetings. Retrieved 21 April 2016.
↑ "Venkatraman Ramakrishnan: Certificate of Election EC/2003/31". London: The Royal Society. 2003. Archived from the original on 18 June 2015. Retrieved 18 June 2015.
↑ Amit Roy (17 Oct 2009). "'Venki' makes light of India link – Winner says not to treat science like cricket; league of misses grows". The Telegraph (Kolkata) . Retrieved 2009-10-17.