Dynamics of Biological Macromolecules: Not a Simple Slaving by Hydration Water

被引:101
|
作者
Khodadadi, S. [3 ]
Roh, J. H. [4 ,5 ,6 ]
Kisliuk, A. [1 ]
Mamontov, E. [2 ]
Tyagi, M. [4 ,6 ]
Woodson, S. A. [5 ]
Briber, R. M. [4 ]
Sokolov, A. P. [1 ,7 ]
机构
[1] Oak Ridge Natl Lab, Div Chem Sci, Oak Ridge, TN 37831 USA
[2] Oak Ridge Natl Lab, Spallat Neutron Source, Oak Ridge, TN USA
[3] Univ Akron, Dept Polymer Sci, Akron, OH 44325 USA
[4] Univ Maryland, Dept Mat Sci & Engn, College Pk, MD 20742 USA
[5] Johns Hopkins Univ, TC Jenkins Dept Biophys, Baltimore, MD USA
[6] Natl Inst Stand & Technol, Ctr Neutron Res, Gaithersburg, MD 20899 USA
[7] Univ Tennessee, Dept Chem, Knoxville, TN 37996 USA
基金
美国国家科学基金会;
关键词
NEUTRON-SCATTERING; PROTEIN DYNAMICS; TRANSFER-RNA; SOLVENT; SPECTROSCOPY; FLUCTUATIONS; TRANSITION; LYSOZYME;
D O I
10.1016/j.bpj.2009.12.4284
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
We studied the dynamics of hydrated tRNA using neutron and dielectric spectroscopy techniques. A comparison of our results with earlier data reveals that the dynamics of hydrated tRNA is slower and varies more strongly with temperature than the dynamics of hydrated proteins. At the same time, tRNA appears to have faster dynamics than DNA. We demonstrate that a similar difference appears in the dynamics of hydration water for these biomolecules. The results and analysis contradict the traditional view of slaved dynamics, which assumes that the dynamics of biological macromolecules just follows the dynamics of hydration water. Our results demonstrate that the dynamics of biological macromolecules and their hydration water depends strongly on the chemical and three-dimensional structures of the biomolecules. We conclude that the whole concept of slaving dynamics should be reconsidered, and that the mutual influence of biomolecules and their hydration water must be taken into account.
引用
收藏
页码:1321 / 1326
页数:6
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