Mayer Kristen L, Earley Matthew R, Gupta Sonia, Pichumani Kumar, Regan Lynne, Stone Martin J
Department of Chemistry, Indiana University, Bloomington, Indiana 47405-0001, USA.
Nat Struct Biol. 2003 Nov;10(11):962-5. doi: 10.1038/nsb991. Epub 2003 Oct 5.
The synchronization (correlation) of conformational fluctuations in folded proteins may influence the rates of enzyme catalysis and ligand binding as well as the stabilities of native proteins and their complexes. However, experimental detection of correlated motions remains difficult. Herein, we present an analysis of the covariation of NMR-derived backbone dynamical parameters among a family of ten mutants of a small protein. Both the spatial restriction and the time scales of backbone motions exhibit a higher degree of covariation than would be expected if the internal motions of each group were independent, providing experimental support for correlated dynamics. Application of this approach to other proteins may reveal dynamical correlations that influence catalysis, ligand-binding and/or protein stability.
折叠蛋白质中构象波动的同步（相关性）可能会影响酶催化和配体结合的速率，以及天然蛋白质及其复合物的稳定性。然而，相关运动的实验检测仍然很困难。在此，我们对一种小蛋白质的十个突变体家族中核磁共振衍生的主链动力学参数的协变进行了分析。与每组内部运动相互独立时的预期情况相比，主链运动的空间限制和时间尺度都表现出更高程度的协变，为相关动力学提供了实验支持。将这种方法应用于其他蛋白质可能会揭示影响催化、配体结合和/或蛋白质稳定性的动力学相关性。
