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Title: Protein dynamics in a broad frequency range: Dielectric spectroscopy studies

Abstract

We present detailed dielectric spectroscopy studies of dynamics in two hydrated proteins, lysozyme and myoglobin. We emphasize the importance of explicit account for possible Maxwell-Wagner (MW) polarization effects in protein powder samples. Combining our data with earlier literature results, we demonstrate the existence of three major relaxation processes in globular proteins. To understand the mechanisms of these relaxations we involve literature data on neutron scattering, simulations and NMR studies. The faster process is ascribed to coupled protein-hydration water motions and has relaxation time similar to 10-50 Ps at room temperature. The intermediate process is similar to 10(2)-10(3) times slower than the faster process and might be strongly affected by MW polarizations. Based on the analysis of data obtained by different experimental techniques and simulations, we ascribe this process to large scale domain-like motions of proteins. The slowest observed process is similar to 10(6)-10(7) times slower than the faster process and has anomalously large dielectric amplitude Delta epsilon similar to 10(2)-10(4). The microscopic nature of this process is not clear, but it seems to be related to the glass transition of hydrated proteins. The presentedresults suggest a general classification of the relaxation processes in hydrated proteins. (c) 2014 Elsevier B.V. Allmore » rights reserved.« less

Authors:
 [1];  [2]
  1. Hebrew Univ. of Jerusalem (Israel)
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Univ. of Tennessee, Knoxville, TN (United States)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1347310
Grant/Contract Number:  
AC05-00OR22725
Resource Type:
Accepted Manuscript
Journal Name:
Journal of Non-Crystalline Solids
Additional Journal Information:
Journal Volume: 407; Journal Issue: C; Journal ID: ISSN 0022-3093
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Protein dynamics; Hydration water; Glass transition; Dielectric spectroscopy; Lysozyme; Myoglobin; EGG-WHITE LYSOZYME; GOLDSTEIN BETA-RELAXATION; BOVINE SERUM-ALBUMIN; NEUTRON SPIN-ECHO; GLOBULAR-PROTEINS; HYDRATION WATER; GLASS FORMERS; PHOSPHOGLYCERATE K

Citation Formats

Nakanishi, Masahiro, and Sokolov, Alexei P. Protein dynamics in a broad frequency range: Dielectric spectroscopy studies. United States: N. p., 2014. Web. doi:10.1016/j.jnoncrysol.2014.08.057.
Nakanishi, Masahiro, & Sokolov, Alexei P. Protein dynamics in a broad frequency range: Dielectric spectroscopy studies. United States. doi:10.1016/j.jnoncrysol.2014.08.057.
Nakanishi, Masahiro, and Sokolov, Alexei P. Wed . "Protein dynamics in a broad frequency range: Dielectric spectroscopy studies". United States. doi:10.1016/j.jnoncrysol.2014.08.057. https://www.osti.gov/servlets/purl/1347310.
@article{osti_1347310,
title = {Protein dynamics in a broad frequency range: Dielectric spectroscopy studies},
author = {Nakanishi, Masahiro and Sokolov, Alexei P.},
abstractNote = {We present detailed dielectric spectroscopy studies of dynamics in two hydrated proteins, lysozyme and myoglobin. We emphasize the importance of explicit account for possible Maxwell-Wagner (MW) polarization effects in protein powder samples. Combining our data with earlier literature results, we demonstrate the existence of three major relaxation processes in globular proteins. To understand the mechanisms of these relaxations we involve literature data on neutron scattering, simulations and NMR studies. The faster process is ascribed to coupled protein-hydration water motions and has relaxation time similar to 10-50 Ps at room temperature. The intermediate process is similar to 10(2)-10(3) times slower than the faster process and might be strongly affected by MW polarizations. Based on the analysis of data obtained by different experimental techniques and simulations, we ascribe this process to large scale domain-like motions of proteins. The slowest observed process is similar to 10(6)-10(7) times slower than the faster process and has anomalously large dielectric amplitude Delta epsilon similar to 10(2)-10(4). The microscopic nature of this process is not clear, but it seems to be related to the glass transition of hydrated proteins. The presentedresults suggest a general classification of the relaxation processes in hydrated proteins. (c) 2014 Elsevier B.V. All rights reserved.},
doi = {10.1016/j.jnoncrysol.2014.08.057},
journal = {Journal of Non-Crystalline Solids},
number = C,
volume = 407,
place = {United States},
year = {2014},
month = {9}
}

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