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Article

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

Journal of molecular biology - 4 Apr 1997

Frisch C, Schreiber G, Johnson C M, Fersht A R

Abstract excerpt

We have studied the thermodynamics of the interaction between the ribonuclease barnase and its natural polypeptide inhibitor barstar. The contribution of specific residues and interactions within the barnase-barstar interface to the enthalpy of binding has been examined using isothermal titration calorimetry and protein engineering. The enthalpy of association of the wild-type proteins is -18.9 (+/-0.1) kcal/mol...

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Identifiers

PMID: 9126847
DOI: 10.1006/jmbi.1997.0892

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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.

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Thermodynamics of the interaction of barnase and barstar: changes in free energy versus changes in enthalpy on mutation.PMID 9126847Read ↗

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Simulation of the diffusional association of barnase and barstar.Semantic proximity Read ↗

A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase.Semantic proximity Read ↗

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

Analysis of protein-protein interactions and the effects of amino acid mutations on their energetics. The importance of water molecules in the binding epitope.Semantic proximity Read ↗

[Stabilizing effect of protein-protein interactions: heat denaturation of barnase and binase complexes with barstar and its C40,82A mutant].Semantic proximity Read ↗

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