Probing protein folding and stability using disulfide bonds

Molecular Biotechnology
N Darby, T E Creighton

Abstract

Disulfide bonds are required to stabilize the folded conformations of many proteins. The rates and equilibria of processes involved in disulfide bond formation and breakage can be manipulated experimentally and can be used to obtain important information about protein folding and stability. A number of experimental procedures for studying these processes, and approaches to interpreting the resulting data, are described here.

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Citations

Sep 14, 2007·The Protein Journal·Changhui YanVasant Honavar
Jul 20, 2005·Pharmaceutical Research·Gary D PipesGerd R Kleemann
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Jun 25, 2010·Journal of the American Chemical Society·Hongkwan Cho, Yan Zhao
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Jul 21, 2009·Biochemistry·Ivan KondovWolfgang Wenzel
Jan 20, 1999·Bioconjugate Chemistry·X ChenV E Anderson
Jul 27, 2017·Biochemistry·Patrick K ChaffeyZhongping Tan

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