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Protein Dynamics on the Nanosecond Time Scale: Dielectric and Simulation Studies

Published

Author(s)

Sheila Khodadadi, Joseph E. Curtis, A. P. Sokolov

Abstract

We studied dynamics of hydrated Rnase A and its hydration shell by combining MD simulations and Dielectric spectroscopy technique. The results show that there are not significant numbers of water molecules at the protein surface which are able to exchange with bulk water on a time scale slower than a few nanoseconds. Detailed analysis of the MD simulations indicate that the observed relaxation process in the tens of nanosecond time range of hydrated protein spectra is mainly caused by protein and involves the entire structure of protein including backbone, side chains and turns. Both surface and the core of the protein are contributing to this motion however surface demonstrates slightly faster dynamics.
Citation
Journal of Physical Chemistry B
Volume
115

Keywords

protein dynamics, molecular dynamics, neutron spin echo

Citation

Khodadadi, S. , Curtis, J. and Sokolov, A. (2011), Protein Dynamics on the Nanosecond Time Scale: Dielectric and Simulation Studies, Journal of Physical Chemistry B, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=906295 (Accessed April 17, 2024)
Created April 21, 2011, Updated October 12, 2021