Protein flexibility reduces solvent-mediated friction barriers of ligand binding to a hydrophobic surface patch
Author:
Affiliation:
1. Theoretical Chemistry
2. Faculty of Chemistry and Biochemistry
3. Ruhr University Bochum
4. D-44780 Bochum
5. Germany
6. School of Molecular Sciences
7. Arizona State University
8. Tempe
9. USA
Abstract
Collective protein-water motion modulates friction for ligands approaching a binding interface.
Funder
Deutsche Forschungsgemeinschaft
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2021/CP/D1CP00181G
Reference53 articles.
1. Interfaces and the driving force of hydrophobic assembly
2. Under water's influence
3. Biological Water: Femtosecond Dynamics of Macromolecular Hydration
4. Water Dynamics in the Hydration Layer around Proteins and Micelles
5. Do we underestimate the importance of water in cell biology?
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1. Dynamics of Hydrogen Bonds between Water and Intrinsically Disordered and Structured Regions of Proteins;The Journal of Physical Chemistry B;2023-09-06
2. Spatially Resolved Hydration Thermodynamics in Biomolecular Systems;The Journal of Physical Chemistry B;2022-05-09
3. Tug-of-War between Internal and External Frictions and Viscosity Dependence of Rate in Biological Reactions;Physical Review Letters;2022-03-07
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