Department of Polymer Science, University of Akron, Akron, Ohio, USA.
Biophys J. 2010 Apr 7;98(7):1321-6. doi: 10.1016/j.bpj.2009.12.4284.
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.
我们使用中子和介电谱技术研究了水合 tRNA 的动力学。将我们的结果与早期数据进行比较表明,水合 tRNA 的动力学比水合蛋白质的动力学更慢,且随温度的变化更大。同时,tRNA 的动力学似乎比 DNA 更快。我们证明,这些生物分子的水合动力学也存在类似的差异。研究结果和分析与传统的从属动力学观点相矛盾,该观点认为生物大分子的动力学只是随水合动力学的变化而变化。我们的研究结果表明,生物大分子及其水合动力学强烈依赖于生物分子的化学和三维结构。我们得出结论,从属动力学的整个概念应该重新考虑,必须考虑生物分子及其水合之间的相互影响。