Atomistic details of protein dynamics and the role of hydration water
Abstract
The importance of protein dynamics for their biological activity is nowwell recognized. Different experimental and computational techniques have been employed to study protein dynamics, hierarchy of different processes and the coupling between protein and hydration water dynamics. But, understanding the atomistic details of protein dynamics and the role of hydration water remains rather limited. Based on overview of neutron scattering, molecular dynamic simulations, NMR and dielectric spectroscopy results we present a general picture of protein dynamics covering time scales from faster than ps to microseconds and the influence of hydration water on different relaxation processes. Internal protein dynamics spread over a wide time range fromfaster than picosecond to longer than microseconds. We suggest that the structural relaxation in hydrated proteins appears on the microsecond time scale, while faster processes present mostly motion of side groups and some domains. Hydration water plays a crucial role in protein dynamics on all time scales. It controls the coupled protein-hydration water relaxation on 10 100 ps time scale. Our process defines the friction for slower protein dynamics. Analysis suggests that changes in amount of hydration water affect not only general friction, but also influence significantly the protein's energy landscape.
- Authors:
-
- Delft Univ. of Technology (Netherlands). Faculty of Applied Sciences and Delft Project Management B.V.
- Univ. of Tennessee, Knoxville, TN (United States). Joint Inst. for Neutron Sciences
- Publication Date:
- Research Org.:
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC); National Science Foundation (NSF)
- OSTI Identifier:
- 1347330
- Grant/Contract Number:
- AC05-00OR22725; DMR-1408811
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Biochimica et Biophysica Acta - General Subjects
- Additional Journal Information:
- Journal Volume: 1861; Journal Issue: PB; Journal ID: ISSN 0304-4165
- Publisher:
- Elsevier
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; protein dynamics; hydration water; energy landscape; neutron scattering; dielectric spectroscopy; MD simulation
Citation Formats
Khodadadi, Sheila, and Sokolov, Alexei P. Atomistic details of protein dynamics and the role of hydration water. United States: N. p., 2016.
Web. doi:10.1016/j.bbagen.2016.04.028.
Khodadadi, Sheila, & Sokolov, Alexei P. Atomistic details of protein dynamics and the role of hydration water. United States. https://doi.org/10.1016/j.bbagen.2016.04.028
Khodadadi, Sheila, and Sokolov, Alexei P. Wed .
"Atomistic details of protein dynamics and the role of hydration water". United States. https://doi.org/10.1016/j.bbagen.2016.04.028. https://www.osti.gov/servlets/purl/1347330.
@article{osti_1347330,
title = {Atomistic details of protein dynamics and the role of hydration water},
author = {Khodadadi, Sheila and Sokolov, Alexei P.},
abstractNote = {The importance of protein dynamics for their biological activity is nowwell recognized. Different experimental and computational techniques have been employed to study protein dynamics, hierarchy of different processes and the coupling between protein and hydration water dynamics. But, understanding the atomistic details of protein dynamics and the role of hydration water remains rather limited. Based on overview of neutron scattering, molecular dynamic simulations, NMR and dielectric spectroscopy results we present a general picture of protein dynamics covering time scales from faster than ps to microseconds and the influence of hydration water on different relaxation processes. Internal protein dynamics spread over a wide time range fromfaster than picosecond to longer than microseconds. We suggest that the structural relaxation in hydrated proteins appears on the microsecond time scale, while faster processes present mostly motion of side groups and some domains. Hydration water plays a crucial role in protein dynamics on all time scales. It controls the coupled protein-hydration water relaxation on 10 100 ps time scale. Our process defines the friction for slower protein dynamics. Analysis suggests that changes in amount of hydration water affect not only general friction, but also influence significantly the protein's energy landscape.},
doi = {10.1016/j.bbagen.2016.04.028},
journal = {Biochimica et Biophysica Acta - General Subjects},
number = PB,
volume = 1861,
place = {United States},
year = {Wed May 04 00:00:00 EDT 2016},
month = {Wed May 04 00:00:00 EDT 2016}
}
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