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

doi:10.1006/jmbi.1997.0892

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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...

Topics

Bacillus
Bacterial Proteins
Calorimetry
Enzyme Inhibitors
Models, Molecular
Mutation
Protein Binding
Protein Engineering
Ribonucleases
Thermodynamics

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