Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering
CHAPTER 5.1: Stabilization of Peptides and Proteins by Engineered Disulfide Bonds
Published:27 Jul 2018
Special Collection: 2018 ebook collectionSeries: Chemical Biology
Douglas B. Craig, Alan A. Dombkowski, 2018. "Stabilization of Peptides and Proteins by Engineered Disulfide Bonds", Oxidative Folding of Proteins: Basic Principles, Cellular Regulation and Engineering, Matthias J Feige
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It is often desirable to increase the stability of proteins. A method for protein stabilization that has been successful in a wide range of applications is disulfide engineering. This method entails the creation of novel disulfide bonds in proteins of interest. An effective approach towards accomplishing this goal is to analyze a structural model of the target protein to identify a residue pair that is oriented in a manner consistent with disulfide formation, then mutate the residues to cysteines. This chapter reviews computational methods that have been developed to assist in disulfide engineering. In addition, a range of successful disulfide engineering applications, from stabilization of industrial enzymes to improvements in vaccine stability and efficacy, are discussed.