Abstract
Among the twenty amino acids that comprise proteins, cysteine has unique properties. It may contribute to protein biological functions by using its sulfhydryl (-SH) group in the active site for enzyme catalysis such as in cysteine proteases, as the chelating site for metal ions, or as the active site of disulfide-reshuffling enzymes (1). The oxidation of sulfhydryl groups to form a disulfide bond is one of the most common posttranslational modifications in proteins. Disulfide bonds play an important role in folding/refolding processes and in maintaining the three-dimensional structure of proteins. The determination of disulfide-bond linkage is therefore an integral part of structural characterization of proteins (2).
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Wu, J., Watson, J.T. (2002). Assignment of Disulfide Bonds in Proteins by Chemical Cleavage and Peptide Mapping by Mass Spectrometry. In: Kannicht, C. (eds) Posttranslational Modifications of Proteins. Methods in Molecular Biology™, vol 194. Humana Press. https://doi.org/10.1385/1-59259-181-7:001
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DOI: https://doi.org/10.1385/1-59259-181-7:001
Publisher Name: Humana Press
Print ISBN: 978-0-89603-678-9
Online ISBN: 978-1-59259-181-7
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