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Article

Thermodynamics of denaturation of mutants of barnase with disulfide crosslinks.

Journal of molecular biology - 25 Apr 1997

Johnson C M, Oliveberg M, Clarke J, Fersht A R

Abstract excerpt

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, but the decreases in the entropy of denaturation are...

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Source

Identifiers

PMID: 9149152
DOI: 10.1006/jmbi.1997.0928

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Thermodynamics of denaturation of mutants of barnase with disulfide crosslinks.PMID 9149152Read ↗

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The kinetic pathway of folding of barnase.Semantic proximity Read ↗

Structural response to mutation at a protein-protein interface.Semantic proximity Read ↗

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Effect of salt on the urea-unfolded form of barstar probed by m value measurements.Semantic proximity Read ↗

Salt bridges in the hyperthermophilic protein Ssh10b are resilient to temperature increases.Semantic proximity Read ↗

Thermodynamics of the interaction of barnase and barstar: changes in free energy versus changes in enthalpy on mutation.Semantic proximity Read ↗

A calorimetric study of the thermal stability of barstar and its interaction with barnase.Semantic proximity Read ↗

Thermodynamic analysis of an antagonistic folding-unfolding equilibrium between two protein domains.Semantic proximity Read ↗

Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme.Semantic proximity Read ↗

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