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Disulfide bonds: determination, location, and influence on molecular properties of proteins

Permanent URL:
http://handle.nal.usda.gov/10113/31252
File:
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Abstract:
Determination and location of cystine residues are essential to protein characterization since their disulfide bonds stabilize chainfolding and multichain structure responsible for physical and biological properties. Reduction with mercaptans, such as dithiothreitol, in dissociating solvents is the choice procedure for attaining disulfide cleavage, since other methods may cause undesirable side reactions. Under selected conditions the resulting sulfhydryls can be specifically alkylated with α,β-unsaturated compounds to prevent their reoxidation. Determination of alkylated cysteine residues supplements the cysteic acid method for cystine-cysteine analysis. Reoxidation studies on reduced proteins indicate that positions of formation of both intra- and interchain disulfide bonds are governed by amino acid sequences as well as by concentration, solvent, and pH. Location of disulfide bonds in peptides obtained by chromatography of proteolytic digests of proteins has been accelerated by automatic analysis with specific reagents. Disulfide interchange may change physical properties of proteins and must be avoided in characterization work.
Author(s):
Wall, J.S.
Note:
Includes references.
Source:
Journal of agricultural and food chemistry July/Aug 1971, 19 (4)
Language:
English
Publisher:
American Chemical Society, Books and Journals Division
Year:
1971
Collection:
Journal Articles, USDA Authors, Peer-Reviewed
Rights:
Works produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted.