Quantification and Location of Disulfide Bonds in Proteins

Sulfhydryl and disulfide groups are of great structural, functional, and biological importance in protein molecules. For example, the Cys sulfhydryl 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 ( 1 ). The conformation of many proteins is stabilized by the presence of disulfide bonds ( 2 ) and the formation of disulfide bonds is an important posttranslational modification of secretory proteins ( 3 ). These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.