A Structure-free Method for Quantifying Conformational Flexibility in proteins.
A Structure-free Method for Quantifying Conformational Flexibility in proteins.
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DOI：
10.1038/srep29040
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发表时间：
2016-06-30
影响因子：
4.6
通讯作者：
Stultz CM
中科院分区：
文献类型：
--
作者：
Burger VM;Arenas DJ;Stultz CM
所有的蛋白质在生理温度下都有一系列的构象，这种固有的灵活性使它们能够执行其规定的功能。因此，对蛋白质功能的全面理解需要蛋白质柔性的表征。在这里，我们描述了一种新的方法，用于量化蛋白质的灵活性，在解决方案中使用小角X射线散射（SAXS）数据。该方法计算有效熵，量化蛋白质在溶液中可以采用的回转半径的多样性，并且不需要显式生成结构集合来获得对蛋白质灵活性的见解。将这种无结构方法应用于200多个实验数据集表明，该方法可以量化蛋白质的紊乱以及配体结合对蛋白质灵活性的影响。这种蛋白质柔性的定量描述形成了蛋白质结构描述和分类的严格分类的基础。
All proteins sample a range of conformations at physiologic temperatures and this inherent flexibility enables them to carry out their prescribed functions. A comprehensive understanding of protein function therefore entails a characterization of protein flexibility. Here we describe a novel approach for quantifying a protein’s flexibility in solution using small-angle X-ray scattering (SAXS) data. The method calculates an effective entropy that quantifies the diversity of radii of gyration that a protein can adopt in solution and does not require the explicit generation of structural ensembles to garner insights into protein flexibility. Application of this structure-free approach to over 200 experimental datasets demonstrates that the methodology can quantify a protein’s disorder as well as the effects of ligand binding on protein flexibility. Such quantitative descriptions of protein flexibility form the basis of a rigorous taxonomy for the description and classification of protein structure.