4b2a

Publication Abstract from PubMed

Abstract The energetics of macromolecular interactions are complex, particularly where protein flexibility is involved. Exploiting serendipitous differences in the plasticity of a series of closely related trypsin variants, we analyzed the enthalpic and entropic contributions accompanying interaction with L45K-eglin C. Binding of the four variants show significant differences in released heat, although the affinities vary little, in accordance with the principle of enthalpy-entropy compensation. Binding of the most disordered variant is almost entirely enthalpically driven, with practically no entropy change. As structures of the complexes reveal negligible differences in protein-inhibitor contacts, we conclude that solvent effects contribute significantly to binding affinities.

Thermodynamic signatures in macromolecular interactions involving conformational flexibility.,Menzel A, Neumann P, Schwieger C, Stubbs MT Biol Chem. 2014 Jul 1;395(7-8):905-11. doi: 10.1515/hsz-2014-0177. PMID:25003391^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.