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Probing protein folding and stability using disulfide bonds.

N Darby·T E Creighton
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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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N Darby, T E Creighton. 1997. Probing protein folding and stability using disulfide bonds.. https://doi.org/10.1007/bf02821544

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