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- Title
On the Molecular Driving Force of Protein–Protein Association.
- Authors
Rapuano, Roberta; Graziano, Giuseppe
- Abstract
The amount of water-accessible-surface-area, WASA, buried upon protein–protein association is a good measure of the non-covalent complex stability in water; however, the dependence of the binding Gibbs free energy change upon buried WASA proves to be not trivial. We assign a precise physicochemical role to buried WASA in the thermodynamics of non-covalent association and perform close scrutiny of the contributions favoring and those contrasting protein–protein association. The analysis indicates that the decrease in solvent-excluded volume, an entropic effect, described by means of buried WASA, is the molecular driving force of non-covalent association in water.
- Subjects
PROTEIN-protein interactions; FREE energy (Thermodynamics); THERMODYNAMICS; CONFORMATIONAL analysis; VOLUMETRIC analysis
- Publication
Biophysica, 2022, Vol 2, Issue 3, p240
- ISSN
2673-4125
- Publication type
Article
- DOI
10.3390/biophysica2030023