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- W1499210328 abstract "Publisher Summary This chapter discusses the basic principles and novel, intriguing applications of mass spectrometry (MS) in quantitative and functional proteomics. In these approaches, capability, versatility, and usefulness of biological MS are exploited at their best. Proteomics takes advantage of the existence of databases containing the sequences of diverse organisms that became available through various genome-sequencing projects. Rapid advancements in mass analyzers and ionization and dissociation methods of biomolecules elevated MS to a key technology in proteomics. Modern proteomics methods combined with MS provide the capability to identify (sub-) cellular proteomes, characterize posttranslational modifications, and map functional protein complexes. In contrast to descriptive proteomics, quantitative proteomics generally identifies only those proteins that show changes in expression levels or undergo changes regarding the relative degree of posttranslational modifications. To attain information on protein abundance, two alternative strategies can be followed. The first one is based on two-dimensional polyacrylamide gel electrophoresis (2-D PAGE), usually followed by single-stage MS for protein identification. The second strategy utilizes MS with or without stable isotope labeling for gaining both qualitative and quantitative information on proteins using the same analytical device. MS-based approaches to quantitative proteomics discussed in the chapter are label-free protein quantification by MS and stable isotope labeling methods for quantitative MS. Obtaining meaningful data in MS-based quantitative proteomics is described in the chapter." @default.
- W1499210328 created "2016-06-24" @default.
- W1499210328 creator A5015935858 @default.
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- W1499210328 date "2008-01-01" @default.
- W1499210328 modified "2023-10-18" @default.
- W1499210328 title "Chapter 17 Mass Spectrometry-Driven Approaches to Quantitative Proteomics and Beyond" @default.
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