Journal
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 4, Issue 6, Pages 936-942Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jz400128u
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Funding
- Scientific User Facilities Division, Office of Basic Energy Sciences, U.S. Department of Energy
- Office of Biological and Environmental Research, US DOE [ERKP291]
- US Department of Energy (DOE) [DE-AC05- 00OR22725]
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The dynamics of RNA within the beta-relaxation region of 10 ps to 1 ns is crucial to its biological function. Because of its simpler chemical building blocks and the lack of the side methyl groups, faster relaxational dynamics of RNA compared to proteins can be expected. However, the situation is actually opposite. In this work, the relaxational dynamics of tRNA is measured by quasielastic neutron scattering and analyzed using the mode coupling theory, originally developed for glass-forming liquids. Our results reveal that the dynamics of tRNA follows a log-decay within the beta-relaxation region, which is an important trait demonstrated by the dynamics of proteins. The dynamics of hydrated tRNA and lysozyme compared in the time domain further demonstrate that the slower dynamics of tRNA relative to proteins originates from the difference in the folded states of tRNA and proteins, as well as the influence of their hydration water.
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