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Protein Conformational Entropy Is Not Slaved To Water, Bryan S Marques, Matthew A Stetz, Christine Jorge, Kathleen G Valentine, A Joshua Wand, Nathaniel V Nucci
Protein Conformational Entropy Is Not Slaved To Water, Bryan S Marques, Matthew A Stetz, Christine Jorge, Kathleen G Valentine, A Joshua Wand, Nathaniel V Nucci
College of Science & Mathematics Departmental Research
Conformational entropy can be an important element of the thermodynamics of protein functions such as the binding of ligands. The observed role for conformational entropy in modulating molecular recognition by proteins is in opposition to an often-invoked theory for the interaction of protein molecules with solvent water. The "solvent slaving" model predicts that protein motion is strongly coupled to various aspects of water such as bulk solvent viscosity and local hydration shell dynamics. Changes in conformational entropy are manifested in alterations of fast internal side chain motion that is detectable by NMR relaxation. We show here that the fast-internal side …