Copied Posttranslational Modification of Proteins
Posttranslational Modification of Proteins
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.
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