通过互相关磁共振弛豫探测固有无序蛋白质中的局部骨架几何形状。
Probing local backbone geometries in intrinsically disordered proteins by cross-correlated NMR relaxation.
机构信息
Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093 Warsaw, Poland.
出版信息
Angew Chem Int Ed Engl. 2013 Apr 22;52(17):4604-6. doi: 10.1002/anie.201210005. Epub 2013 Mar 20.
Abstract
An ultra-high-resolution NMR experiment for the measurement of intraresidue (1)H(i)-(15)N(i)-(13)C'(i) dipolar-chemical shift anisotropy relaxation interference is employed to extract information about local backbone geometries in intrinsically disordered proteins. The study of tumor suppressor BASP1 revealed a population shift of β-turn geometries at low pH conditions and a compaction of the BASP1 structural ensemble.
摘要
采用超高分辨率 NMR 实验测量残基内 (1)H(i)-(15)N(i)-(13)C'(i) 二极偶-化学位移各向异性弛豫干扰，以提取固有无序蛋白质中局部骨架几何形状的信息。对肿瘤抑制因子 BASP1 的研究表明，在低 pH 条件下，β-转角几何形状发生了种群转移，BASP1 结构集合发生了紧缩。
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