A simple method to predict protein flexibility using secondary chemical shifts
A simple method to predict protein flexibility using secondary chemical shifts
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DOI：
10.1021/ja054842f
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发表时间：
2005-11-02
影响因子：
15
通讯作者：
Wishart, DS
中科院分区：
文献类型：
--
作者：
Berjanskii, MV;Wishart, DS
蛋白质运动在许多生物过程中起着至关重要的作用，如酶催化、变构调节、抗原-抗体相互作用和蛋白质- DNA结合。核磁共振波谱在研究蛋白质动力学的方法中占有独特的地位，因为它能够在大范围的时间尺度上提供关于蛋白质运动的特定位点信息。然而，大多数核磁共振方法需要详细了解3D结构和/或收集额外的实验数据（NOEs, T1， T2等）以准确测量蛋白质动力学。在这里，我们提出了一种基于化学位移数据的简单方法，该方法可以精确，定量，位点特异性地绘制蛋白质骨干迁移率，而不需要三维结构或NMR弛豫数据的收集和分析。此外，我们表明，这种化学位移方法能够定量预测每残基RMSD值（从MD模拟和核磁共振结构集成）以及无模型主干顺序参数。
Protein motions play a critical role in many biological processes, such as enzyme catalysis, allosteric regulation, antigen−antibody interactions, and protein−DNA binding. NMR spectroscopy occupies a unique place among methods for investigating protein dynamics due to its ability to provide site-specific information about protein motions over a large range of time scales. However, most NMR methods require a detailed knowledge of the 3D structure and/or the collection of additional experimental data (NOEs, T1, T2, etc.) to accurately measure protein dynamics. Here we present a simple method based on chemical shift data that allows accurate, quantitative, site-specific mapping of protein backbone mobility without the need of a three-dimensional structure or the collection and analysis of NMR relaxation data. Further, we show that this chemical shift method is able to quantitatively predict per-residue RMSD values (from both MD simulations and NMR structural ensembles) as well as model-free backbone order parameters.