Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, UJF, UMR 5075, 41 Rue Jules Horowitz, Grenoble 38027, France.
J Am Chem Soc. 2010 Feb 3;132(4):1270-2. doi: 10.1021/ja909973n.
The development of meaningful descriptions of the conformational behavior of intrinsically disordered proteins represents a key challenge for contemporary structural biology. An approach is developed, based on the combination of ensemble descriptions of unfolded proteins and state-of-the-art chemical shift prediction algorithms, to describe backbone dihedral angle conformational behavior on the basis of (13)C and (15)N NMR chemical shifts alone. This allows the identification and characterization of entire secondary structural elements and their associated populations, as well as providing indications of the subtle detail of local conformational sampling in unfolded proteins.
发展对无规卷曲蛋白质构象行为的有意义描述是当代结构生物学面临的一项关键挑战。本文提出了一种方法，它基于无规卷曲蛋白质的集合描述与最先进的化学位移预测算法相结合，仅根据 (13)C 和 (15)N NMR 化学位移来描述主链二面角构象行为。这可以识别和描述整个二级结构元件及其相关的丰度，并提供无规卷曲蛋白质中局部构象采样的细微细节的指示。
