Abstract
Publisher Summary This chapter discusses strategies for locating disulfide bonds in proteins. Disulfide bonding in proteins is one of the most frequently encountered posttranslational modifications of proteins. Because of the important role played by disulfide bonds in establishing and maintaining the three-dimensional character of proteins, it is important to know whether a protein or peptide contains disulfide bonds, and, for proteins that contain more than two half-cystinyl residues, it is important to know which residues are joined by disulfide bonds. Disulfide cross-linkages may be located by cleaving a protein between half-cystinyl residues to give peptides that contain only one disulfide bond. The molecular weights of these peptides are determined by fast atom bombardment mass spectrometry (FAB-MS) and related to specific segments of the parent protein. This latter step, identification of the disulfide-containing peptide, is facilitated greatly if a cleavage reagent that cleaves the protein at specific sites is used. Proteins may be cleaved selectively with a variety of enzymes, such as trypsin, chymotrypsin, Staphylococcus aureus V8, or pepsin.
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