Interpreting dynamically-averaged scalar couplings in proteins
Interpreting dynamically-averaged scalar couplings in proteins
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DOI：
10.1007/s10858-005-8873-0
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发表时间：
2005-08-01
影响因子：
2.7
通讯作者：
Vendruscolo, M
中科院分区：
文献类型：
--
作者：
Lindorff-Larsen, K;Best, RB;Vendruscolo, M
标量三键耦合常数的实验测定是探测蛋白质结构和动力学的有力方法。这种耦合常数的详细结构解释通常基于Karplus关系，其允许测量的耦合与分子的扭转角相关。由于测得的耦合是敏感的热波动，在Karplus关系中的参数是更好地来自合奏代表的二面角的分布存在于解决方案中，而不是从单一的构象。我们提出了一种方法来获得这样的参数，使用合奏的构象确定通过动态合奏细化-一种方法，提供结构合奏，同时代表蛋白质的结构和相关的动态。
The experimental determination of scalar three-bond coupling constants represents a powerful method to probe both the structure and dynamics of proteins. The detailed structural interpretation of such coupling constants is usually based on Karplus relationships, which allow the measured couplings to be related to the torsion angles of the molecules. As the measured couplings are sensitive to thermal fluctuations, the parameters in the Karplus relationships are better derived from ensembles representing the distributions of dihedral angles present in solution, rather than from single conformations. We present a method to derive such parameters that uses ensembles of conformations determined through dynamic-ensemble refinement - a method that provides structural ensembles that simultaneously represent both the structure and the associated dynamics of a protein.