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蛋白质中连续的 C'-N 基团的直接相关性：一种用于鉴定固有无序蛋白质的方法。

Direct correlation of consecutive C'-N groups in proteins: a method for the assignment of intrinsically disordered proteins.

机构信息

Instituto de Química Física Rocasolano, CSIC, Serrano 119, 28006, Madrid, Spain.

出版信息

J Biomol NMR. 2013 Sep;57(1):57-63. doi: 10.1007/s10858-013-9765-3. Epub 2013 Aug 9.

DOI:10.1007/s10858-013-9765-3
PMID:23929272
Abstract

Two novel 3D (13)C-detected experiments, hNcocaNCO and hnCOcaNCO, are proposed to facilitate the resonance assignment of intrinsically disordered proteins. The experiments correlate the (15)N and (13)C' chemical shifts of two consecutive amide moieties without involving other nuclei, thus taking advantage of the good dispersion shown by the (15)N-(13)C' correlations, even for proteins that lack a well defined tertiary structure. The new pulse sequences were successfully tested using Nupr1, an intrinsically disordered protein of 93 residues.

摘要

提出了两种新的 3D (13)C 检测实验，hncocaNCO 和 hnCOcaNCO，以方便对固有无序蛋白质进行共振分配。这些实验通过不涉及其他核的方式，将两个连续酰胺基团的 (15)N 和 (13)C'化学位移关联起来，从而利用 (15)N-(13)C'相关性的良好分散性，即使对于缺乏明确定义的三级结构的蛋白质也是如此。使用 93 个残基的固有无序蛋白 Nupr1 成功测试了新的脉冲序列。

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