Document Type
Article
Version Deposited
Published Version
Publication Date
10-16-2020
Publication Title
Scientific Reports
DOI
10.1038/s41598-020-74382-5
Abstract
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 chain dynamics of several proteins are unaffected by changes to the hydration layer and bulk water. These observations indicate that the participation of conformational entropy in protein function is not dictated by the interaction of protein molecules and solvent water under the range of conditions normally encountered.
Recommended Citation
Marques, B.S., Stetz, M.A., Jorge, C., Valentine, K.G., Wand, A.J. & Nucci, N.V. (2020). Protein conformational entropy is not slaved to water. Scientific Reports 10, 17587 (2020).
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Comments
Open Access. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.