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Updated: Jun 24, 2026
Designing Silk-silk Protein Alloy Materials for Biomedical Applications
Published on: August 13, 2014
An enthalpic component in cooperativity: the relationship between enthalpy, entropy, and noncovalent structure in
1Cambridge Centre for Molecular Recognition, University Chemical Laboratory, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom.
Abstract:
Attempts to quantify binding interactions of noncovalent complexes in aqueous solution have been stymied by complications arising from enthalpy-entropy compensation and cooperativity. We have extended work detailing the relationship between noncovalent structure and free energy of binding to include the roles of enthalpy and entropy of association. On the basis of van't Hoff measurements of the dimerization of vancomycin type antibiotics, we demonstrate that positive cooperativity manifests itself in a more favorable enthalpy of association and a partially compensating less favorable entropy of association. Finally, we extend these results to rationalize thermodynamic observations in unrelated systems.
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