Protein and solvent dynamics: How strongly are they coupled?

被引：131

作者：

Caliskan, G ^{[1
]}

Mechtani, D

Roh, JH

Kisliuk, A

Sokolov, AP

Azzam, S

Cicerone, MT

Lin-Gibson, S

Peral, I

机构：

[1] Univ Akron, Dept Polymer Sci, Akron, OH 44325 USA

[2] Natl Inst Stand & Technol, Gaithersburg, MD 20899 USA

[3] Kent State Univ, Dept Chem, Kent, OH 44242 USA

[4] Univ Maryland, Dept Mat Sci & Engn, College Pk, MD 20742 USA

来源：

JOURNAL OF CHEMICAL PHYSICS | 2004年 / 121卷 / 04期

关键词：

D O I：

10.1063/1.1764491

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Analysis of Raman and neutron scattering spectra of lysozyme demonstrates that the protein dynamics follow the dynamics of the solvents glycerol and trehalose over the entire temperature range measured 100-350 K. The protein's fast conformational fluctuations and low-frequency vibrations and their temperature variations are very sensitive to behavior of the solvents. Our results give insight into previous counterintuitive observations that protein relaxation is stronger in solid trehalose than in liquid glycerol. They also provide insight into the effectiveness of glycerol as a biological cryopreservant. (C) 2004 American Institute of Physics.

引用

页码：1978 / 1983

页数：6

共 40 条

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