Matthias Mann, is a scientist in the area of mass spectrometry and proteomics, he received his Ph.D. in 1988 at Yale University where he worked in the group of who, which American research professor of analytical chemistry who was awarded a share of the Nobel Prize in Chemistry in 2002?
John Fenn
Matthias Mann
Matthias Mann (born 10 October 1959) is a scientist in the area of mass spectrometry and proteomics.
 Born in Germany he studied mathematics and physics at the University of Göttingen.
 He received his Ph.D. in 1988 at Yale University where he worked in the group of John Fenn, who was later awarded the Nobel Prize in Chemistry.
 After a postdoctoral fellowship at the University of Southern Denmark in Odense he became group leader at the European Molecular Biology Laboratory (EMBL) in Heidelberg.
 Later he went back to Odense as a professor of bioinformatics.
 Since 2005 he has been a director at the Max Planck Institute of Biochemistry in Munich.
 In addition, he will also become a principal investigator at the newly founded "Novo Nordisk Foundation Center for Protein Research" in Copenhagen.
John Fenn (chemist)
John Bennett Fenn (June 15, 1917December 10, 2010) was an American research professor of analytical chemistry who was awarded a share of the Nobel Prize in Chemistry in 2002.
 Fenn shared half of the award with Koichi Tanaka for their work in mass spectrometry.
 The other half of the 2002 award went to Kurt Wüthrich.
 Fenn's contributions specifically related to the development of electrospray ionization, now a commonly used technique for large molecules and routine liquid chromatography-tandem mass spectrometry.
 Early in his career, Fenn did research in the field of jet propulsion at Project SQUID, and focused on molecular beam studies.
 Fenn finished his career with more than 100 publications, including one book.
Ion-mobility spectrometry–mass spectrometry
Ion-mobility spectrometry–mass spectrometry (IMS-MS), also known as ion-mobility separation–mass spectrometry, is an analytical chemistry method that separates gas phase ions on a millisecond timescale using ion-mobility spectrometry and uses mass spectrometry on a microsecond timescale to identify components in a sample. Time-resolved mass spectrometry
Time-resolved mass spectrometry (TRMS) is a strategy in analytical chemistry that uses mass spectrometry platform to collect data with temporal resolution.
 Implementation of TRMS builds on the ability of mass spectrometers to process ions within sub-second duty cycles.
 It often requires the use of customized experimental setups.
 However, they can normally incorporate commercial mass spectrometers.
 As a concept in analytical chemistry TRMS encompasses instrumental developments (e.g. interfaces, ion sources, mass analyzers), methodological developments, and applications. Capillary electrophoresis–mass spectrometry
Capillary electrophoresis–mass spectrometry (CE-MS) is an analytical chemistry technique formed by the combination of the liquid separation process of capillary electrophoresis with mass spectrometry.
 CE-MS combines advantages of both CE and MS to provide high separation efficiency and molecular mass information in a single analysis.
 It has high resolving power and sensitivity, requires minimal volume and can analyze at high speed.
 Ions are typically formed by electrospray ionization, but they can also be formed by matrix-assisted laser desorption/ionization or other ionization techniques.
 It has applications in basic research in proteomics and quantitative analysis of biomolecules as well as in clinical medicine. David E. Clemmer
David E. Clemmer (February 23, 1965, Alamosa, Colorado -) is an analytical chemist and the Distinguished Professor and Robert and Marjorie Mann Chair of Chemistry at Indiana University in Bloomington, Indiana, where he leads the Clemmer Group.
 Clemmer develops new scientific instruments for ion mobility mass spectrometry (MS), including the first instrument for nested ion-mobility time-of-flight mass spectrometry.
 He has received a number of awards, including the Biemann Medal in 2006 "for his pioneering contributions to the integration of ion mobility separations with a variety of mass spectrometry technologies." Mass spectrometry data format
Mass spectrometry is a scientific technique for measuring the mass to charge ratio of ions.
 It is often coupled to chromatographic techniques such as gas- or liquid chromatography and has found widespread adoption in the fields of analytical chemistry and biochemistry where it can be used to identify and characterize small molecules and proteins (proteomics).
 The large volume of data produced in a typical mass spectrometry experiment requires that computers be used for data storage and processing.
 Over the years, different manufacturers of mass spectrometers have developed various proprietary data formats for handling such data which makes it difficult for academic scientists to directly manipulate their data.
 To address this limitation, several open, XML-based data formats have recently been developed by the Trans-Proteomic Pipeline at the Institute for Systems Biology to facilitate data manipulation and innovation in the public sector.
 These data formats are described here. Analytical and Bioanalytical Chemistry
Analytical and Bioanalytical Chemistry is a peer-reviewed scientific journal publishing research articles in the broad field of analytical and bioanalytical chemistry.
 Some of the subjects covered are the development of instruments for mass spectrometry, metallomics, ionics, and the analytical characterization of nano- and biomaterials.
 The journal was first published in 1862 under the name Fresenius’ Journal of Analytical Chemistry.
 In 2002 the journal was renamed to "Analytical and Bioanalytical Chemistry". Liquid chromatography–mass spectrometry
Liquid chromatography–mass spectrometry (LC-MS) is an analytical chemistry technique that combines the physical separation capabilities of liquid chromatography (or HPLC) with the mass analysis capabilities of mass spectrometry (MS).
 Coupled chromatography - MS systems are popular in chemical analysis because the individual capabilities of each technique are enhanced synergistically.
 While liquid chromatography separates mixtures with multiple components, mass spectrometry provides structural identity of the individual components with high molecular specificity and detection sensitivity.
 This tandem technique can be used to analyze biochemical, organic, and inorganic compounds commonly found in complex samples of environmental and biological origin.
 Therefore, LC-MS may be applied in a wide range of sectors including biotechnology, environment monitoring, food processing, and pharmaceutical, agrochemical, and cosmetic industries. Quantitative proteomics
Quantitative proteomics is an analytical chemistry technique for determining the amount of proteins in a sample.
 Rather than just providing lists of proteins identified in a certain sample, quantitative proteomics yields information about differences between samples.
 For example, this approach can be used to compare samples from healthy and diseased patients.
 The methods for protein identification are identical to those used in general (i.e. qualitative) proteomics, but include quantification as an additional dimension.
 Quantitative proteomics is mainly performed by two-dimensional gel electrophoresis (2-DE) or mass spectrometry (MS).
 However, a recent developed method of Quantitative Dot Blot (QDB) analysis is able to measure both the absolute and relative quantity of an individual proteins in the sample in high throughput format, thus open a new direction for proteomic research.
 In contrast to 2-DE, which requires MS for the downstream protein identification, MS technology can identify and quantify the changes.