Abstract
Sulfydryl and disulfide groups are of great structural, functional, and biological importance in protein molecules. For example, the Cys sulfydryl is essential for the catalytic activity of some enzymes (e.g., thiol proteases) and the interconversion of Cys SH to cystine S-S is directly involved in the activity of protein disulfide isomerase. The conformation of many proteins is stabilized by the presence of disulfide bonds (1) and the formation of disulfide bonds is an important post-translational modification of secretory proteins.
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Aitken, A., Learmonth, M. (2003). Quantitation and Location of Disulfide Bonds in Proteins. In: Smith, B.J. (eds) Protein Sequencing Protocols. Methods in Molecular Biology™, vol 211. Humana Press. https://doi.org/10.1385/1-59259-342-9:399
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DOI: https://doi.org/10.1385/1-59259-342-9:399
Publisher Name: Humana Press
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