Springer Protocols: Abstract: Identification of Proteins Based on MS/MS Spectra and Location of Posttranslational Modifications

Identification of Proteins Based on MS/MS Spectra and Location of Posttranslational Modifications

By: Kathryn L. Stone², Myron Crawford², Walter McMurray², Nancy Williams², Kenneth R. Williams²

Abstract

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Comparative protein profiling is a key approach to understanding the human and other proteomes. Systems-level profiling technologies, such as differential fluorescence twodimensional gel electrophoresis (DIGE), often require the identification of the proteins that are contained within 50 or more spots per gel. A major focus of this chapter therefore is devoted to a general approach for high throughput protein identification that is based on liquid chromatography (LC)/tandem mass spectrometry (MS/MS) analysis of tryptic digests of individual proteins or mixtures of only a few proteins (i.e., as are usually obtained from individual DIGE spots), and that is also applicable to the analysis of complex protein extracts. Additionally, multiple techniques will be described for identifying sites of protein posttranslational modification, with emphasis on phosphorylation and Arg methylation.

Affiliation(s): (2) WM Keck Foundation Biotechnology Resource Laboratory, Mass Spectrometry and Protomic Resources, Yale University, New Haven, CT

Book Title: Peptide Characterization and Application Protocols

Series: Methods in Molecular Biology | Volume: 386 | Pub. Date: May-11-2007 | Page Range: 57-77 | DOI: 10.1007/978-1-59745-430-8_2

Subject: Protein Science

Key Words: MS/MS - phosphorylation - methylation

References

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