Thermodynamics of denaturation of mutants of barnase with disulfide crosslinks.

Abstract

We have measured the effects of disulfide crosslinks on the thermodynamics of denaturation of three mutants of barnase that contain cystine and the corresponding single and double cysteine mutants. At first sight, the data are consistent with the hypothesis that disulfide crosslinks stabilise proteins through entropic destabilisation of the denatured state… (More)

Topics

Cite this paper

@article{Johnson1997ThermodynamicsOD, title={Thermodynamics of denaturation of mutants of barnase with disulfide crosslinks.}, author={C. M. Johnson and Mikael Oliveberg and JL. Clarke and A. R. Fersht}, journal={Journal of molecular biology}, year={1997}, volume={268 1}, pages={198-208} }