Protein-Protein Interfaces Probed by Methyl Labeling and Proton-Detected Solid-State NMR Spectroscopy

被引：9

作者：

Zinke, Maximilian ^{[1
]}

Fricke, Pascal ^{[1
]}

Lange, Sascha ^{[1
]}

Zinn-Justin, Sophie ^{[3
]}

Lange, Adam ^{[1
,2
]}

机构：

[1] Leibniz Forschungsinst Mol Pharmakol FMP, Dept Mol Biophys, Berlin, Germany

[2] Humboldt Univ, Inst Biol, Berlin, Germany

[3] Univ Paris Saclay, Univ Paris Sud, Inst Integrat Biol Cell I2BC, CEA,CNRS, Gif Sur Yvette, France

来源：

CHEMPHYSCHEM | 2018年 / 19卷 / 19期

基金：

欧洲研究理事会;

关键词：

methyl labeling; interfaces; proteins; protein structures; solid-state NMR; H-1-H-1 DISTANCE RESTRAINTS; MULTIDIMENSIONAL NMR; RESONANCE ASSIGNMENT; BACKBONE ASSIGNMENT; FIBRILS; ISOLEUCINE; C-13;

D O I：

10.1002/cphc.201800542

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Proton detection and fast magic-angle spinning have advanced biological solid-state NMR, allowing for the backbone assignment of complex protein assemblies with high sensitivity and resolution. However, so far no method has been proposed to detect intermolecular interfaces in these assemblies by proton detection. Herein, we introduce a concept based on methyl labeling that allows for the assignment of these moieties and for the study of protein-protein interfaces at atomic resolution.

引用

页码：2457 / 2460

页数：4

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