Apparent decoupling of the dynamics of a protein from the dynamics of its aqueous solvent

Xiang Qiang Chu; Eugene Mamontov; Hugh O'Neill; Qiu Zhang

doi:10.1021/jz201435q

Apparent decoupling of the dynamics of a protein from the dynamics of its aqueous solvent

Xiang Qiang Chu, Eugene Mamontov, Hugh O'Neill, Qiu Zhang

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23 Scopus citations

Abstract

Studies of the low-temperature dynamics of proteins in aqueous solutions are limited by the crystallization of water. In this work, we use a solution of LiCl in D ₂O as a solvent for a protein to prevent crystallization and study the dynamics of both the protein and its aqueous solvent by quasielastic neutron scattering (QENS) in the temperature range of 210 to 290 K. Our results reveal that, while the dynamics of the aqueous solvent undergoes a crossover at about 220 K, the dynamics of the protein itself shows no transition at this temperature. The prevailing view is that the β-fluctuations of the protein are governed by the α-fluctuations of the solvent; therefore, observation of the apparent decoupling between the dynamics of the protein and its solvent below the crossover temperature is remarkable.

Original language	English
Pages (from-to)	380-385
Number of pages	6
Journal	Journal of Physical Chemistry Letters
Volume	3
Issue number	3
DOIs	https://doi.org/10.1021/jz201435q
State	Published - Feb 2 2012

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abstract = "Studies of the low-temperature dynamics of proteins in aqueous solutions are limited by the crystallization of water. In this work, we use a solution of LiCl in D 2O as a solvent for a protein to prevent crystallization and study the dynamics of both the protein and its aqueous solvent by quasielastic neutron scattering (QENS) in the temperature range of 210 to 290 K. Our results reveal that, while the dynamics of the aqueous solvent undergoes a crossover at about 220 K, the dynamics of the protein itself shows no transition at this temperature. The prevailing view is that the β-fluctuations of the protein are governed by the α-fluctuations of the solvent; therefore, observation of the apparent decoupling between the dynamics of the protein and its solvent below the crossover temperature is remarkable.",

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AU - Zhang, Qiu

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AB - Studies of the low-temperature dynamics of proteins in aqueous solutions are limited by the crystallization of water. In this work, we use a solution of LiCl in D 2O as a solvent for a protein to prevent crystallization and study the dynamics of both the protein and its aqueous solvent by quasielastic neutron scattering (QENS) in the temperature range of 210 to 290 K. Our results reveal that, while the dynamics of the aqueous solvent undergoes a crossover at about 220 K, the dynamics of the protein itself shows no transition at this temperature. The prevailing view is that the β-fluctuations of the protein are governed by the α-fluctuations of the solvent; therefore, observation of the apparent decoupling between the dynamics of the protein and its solvent below the crossover temperature is remarkable.

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Apparent decoupling of the dynamics of a protein from the dynamics of its aqueous solvent

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