Posttranslational Modification of Proteins: Tools for Functional Proteomics (Methods in Molecular Biology, 194)

Posttranslational Modifications of Proteins: Tools for Functional Proteomics is a compilation of detailed protocols needed to detect and analyze the most important co- and posttranslational modifications of proteins. Though, for reasons of simplicity not explicitly mentioned in the title, both kinds of modifications are covered, whether they occur during, or after, biosynthesis of the protein. My intention was to cover the most significant protein modifications, focusing on the fields of protein function, proteome research, and the characterization of pharmaceutical proteins. The majority of all proteins undergo co- and/or posttranslational modifications. Knowledge of these modifications is extremely important, since they may alter physical and chemical properties, folding, conformation distribution, stability, act- ity, and, consequently, function of the proteins. Moreover, the modification itself can act as an added functional group. Examples of the biological effects of protein mo- fications include: phosphorylation for signal transduction, ubiquitination for p- teolysis, attachment of fatty acids for membrane anchoring or association, glycosylation for protein half-life, targeting, cell-cell and cell-matrix interactions, and carboxylation in protein-ligand binding to name just a few. Full understanding of a specific protein structure-function relationship requires detailed information not only on its amino acid sequence, which is determined by the corresponding DNA sequence, but also on the presence and structure of protein modifications.

The majority of all proteins undergo posttranslational modifications that significantly alter their physical and chemical properties, including their folding and conformation distribution, their stability, and, consequently, their activity and function. In Posttranslational Modifications of Proteins: Tools for Functional Proteomics, Christoph Kannicht and a panel of highly experienced researchers describe readily reproducible methods for detecting and analyzing the most important of these modifications, particularly with regard to protein function, proteome research, and the characterization of pharmaceutical proteins. Among the methods presented are those for analyzing the assignment of disulfide bond sites in proteins, protein N-glycosylation and protein O-glycosylation, and oligosaccharides present at specific single glycosylation sites in a protein. Additional powerful techniques facilitate the analysis of glycosylphosphatidylinositols, lipid modifications, protein phosphorylation and sulfation, protein methylation and acetylation, a-amidation, g-glutamate, isoaspartate, and lysine hydroxylation.
Comprehensive and state-of-the-art, Posttranslational Modifications of Proteins: Tools for Functional Proteomics serves as a highly practical guide for all investigators of protein structure-function relationships not only in chemical and pharmaceutical research, but also throughout the rapidly growing field of functional proteomics.