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Dynamics of Biological Macromolecules: Not a Simple Slaving by Hydration Water |
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| Authors: | S Khodadadi A Kisliuk M Tyagi SA Woodson AP Sokolov |
| Institution: | † Department of Polymer Science, University of Akron, Akron, Ohio ‡ Department of Materials Science and Engineering, University of Maryland, College Park, Maryland § T. C. Jenkins Department of Biophysics, The Johns Hopkins University, Baltimore, Maryland ¶ Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland ‖ Chemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee †† Spallation Neutron Source, Oak Ridge National Laboratory, Oak Ridge, Tennessee ‡‡ Department of Chemistry, University of Tennessee, Knoxville, Tennessee |
| Abstract: | 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. |
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