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.
