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Title: Microscopic relaxations in a protein sustained down to 160 K in a non-glass forming organic solvent

Abstract

In this paper, we have studied microscopic dynamics of a protein in carbon disulfide, a non-glass forming solvent, down to its freezing temperature of ca. 160 K. We have utilized quasielastic neutron scattering. A comparison of lysozyme hydrated with water and dissolved in carbon disulfide reveals a stark difference in the temperature dependence of the protein's microscopic relaxation dynamics induced by the solvent. In the case of hydration water, the common protein glass-forming solvent, the protein relaxation slows down in response to a large increase in the water viscosity on cooling down, exhibiting a well-known protein dynamical transition. The dynamical transition disappears in non-glass forming carbon disulfide, whose viscosity remains a weak function of temperature all the way down to freezing at just below 160 K. The microscopic relaxation dynamics of lysozyme dissolved in carbon disulfide is sustained down to the freezing temperature of its solvent at a rate similar to that measured at ambient temperature. Finally, our results demonstrate that protein dynamical transition is not merely solvent-assisted, but rather solvent-induced, or, more precisely, is a reflection of the temperature dependence of the solvent's glass-forming dynamics.

Authors:
 [1];  [1]
  1. ORNL
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)
OSTI Identifier:
1337815
Alternate Identifier(s):
OSTI ID: 1396440
Grant/Contract Number:  
AC05-00OR22725
Resource Type:
Accepted Manuscript
Journal Name:
Biochimica et Biophysica Acta - General Subjects
Additional Journal Information:
Journal Volume: 1861; Journal Issue: 1B; Journal ID: ISSN 0304-4165
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY

Citation Formats

Mamontov, Eugene, and O'Neil, Hugh. Microscopic relaxations in a protein sustained down to 160 K in a non-glass forming organic solvent. United States: N. p., 2016. Web. https://doi.org/10.1016/j.bbagen.2016.04.024.
Mamontov, Eugene, & O'Neil, Hugh. Microscopic relaxations in a protein sustained down to 160 K in a non-glass forming organic solvent. United States. https://doi.org/10.1016/j.bbagen.2016.04.024
Mamontov, Eugene, and O'Neil, Hugh. Tue . "Microscopic relaxations in a protein sustained down to 160 K in a non-glass forming organic solvent". United States. https://doi.org/10.1016/j.bbagen.2016.04.024. https://www.osti.gov/servlets/purl/1337815.
@article{osti_1337815,
title = {Microscopic relaxations in a protein sustained down to 160 K in a non-glass forming organic solvent},
author = {Mamontov, Eugene and O'Neil, Hugh},
abstractNote = {In this paper, we have studied microscopic dynamics of a protein in carbon disulfide, a non-glass forming solvent, down to its freezing temperature of ca. 160 K. We have utilized quasielastic neutron scattering. A comparison of lysozyme hydrated with water and dissolved in carbon disulfide reveals a stark difference in the temperature dependence of the protein's microscopic relaxation dynamics induced by the solvent. In the case of hydration water, the common protein glass-forming solvent, the protein relaxation slows down in response to a large increase in the water viscosity on cooling down, exhibiting a well-known protein dynamical transition. The dynamical transition disappears in non-glass forming carbon disulfide, whose viscosity remains a weak function of temperature all the way down to freezing at just below 160 K. The microscopic relaxation dynamics of lysozyme dissolved in carbon disulfide is sustained down to the freezing temperature of its solvent at a rate similar to that measured at ambient temperature. Finally, our results demonstrate that protein dynamical transition is not merely solvent-assisted, but rather solvent-induced, or, more precisely, is a reflection of the temperature dependence of the solvent's glass-forming dynamics.},
doi = {10.1016/j.bbagen.2016.04.024},
journal = {Biochimica et Biophysica Acta - General Subjects},
number = 1B,
volume = 1861,
place = {United States},
year = {2016},
month = {5}
}

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Cited by: 2 works
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