Quantitative proteomics in biological research
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|Title:||Quantitative proteomics in biological research||Authors:||Wilm, Matthias||Permanent link:||http://hdl.handle.net/10197/4247||Date:||Oct-2009||Abstract:||Proteomics has enabled the direct investigation of biological material, at first through the analysis of individual proteins, then of lysates from cell cultures, and finally of extracts from tissues and biopsies from entire organisms. Its latest manifestation - quantitative proteomics - allows deeper insight into biological systems. This article reviews the different methods used to extract quantitative information from mass spectra. It follows the technical developments aimed toward global proteomics, the attempt to characterize every expressed protein in a cell by at least one peptide. When applications of the technology are discussed, the focus is placed on yeast biology. In particular, differential quantitative proteomics, the comparison between an experiment and its control, is very discriminating for proteins involved in the process being studied. When trying to understand biological processes on a molecular level, differential quantitative proteomics tends to give a clearer picture than global transcription analyses. As a result, MS has become an even more indispensable tool for biochemically motivated biological research.||Type of material:||Journal Article||Publisher:||Wiley||Copyright (published version):||2009 WILEY-VCH Verlag GmbH & Co.||Keywords:||MS; Protein interaction; Affinity chromatography; Proteomics methods; Functional proteomics; Cell biology||DOI:||10.1002/pmic.200900299||Language:||en||Status of Item:||Peer reviewed|
|Appears in Collections:||Conway Institute Research Collection|
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