Measurement of backbone hydrogen-deuterium exchange in the type III secretion system needle protein PrgI by solid-state NMR

被引：5

作者：

Chevelkov, Veniamin ^{[1
]}

Giller, Karin ^{[2
]}

Becker, Stefan ^{[2
]}

Lange, Adam ^{[1
,3
]}

机构：

[1] Leibniz Forschungsinst Mol Pharmakol, Dept Mol Biophys, D-13125 Berlin, Germany

[2] Max Planck Inst Biophys Chem, Dept NMR Based Struct Biol, D-37077 Gottingen, Germany

[3] Humboldt Univ, Inst Biol, D-10115 Berlin, Germany

来源：

JOURNAL OF MAGNETIC RESONANCE | 2017年 / 283卷

基金：

欧洲研究理事会;

关键词：

Magic-angle spinning solid-state NMR; Relax-EXSY; H/D exchange; Deuteration; Amide protons; Proton detection; PrgI; Relaxation; PANCREATIC TRYPSIN-INHIBITOR; AMIDE PROTON-EXCHANGE; SENSITIVITY ENHANCEMENT; POLARIZATION TRANSFER; QUANTITATIVE-ANALYSIS; AMYLOID FIBRILS; H/D EXCHANGE; RATES; SPECTROSCOPY; RESOLUTION;

D O I：

10.1016/j.jmr.2017.08.012

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

In this report we present site-specific measurements of amide hydrogen-deuterium exchange rates in a protein in the solid state phase by MAS NMR. Employing perdeuteration, proton detection and a high external magnetic field we could adopt the highly efficient Relax-EXSY protocol previously developed for liquid state NMR. According to this method, we measured the contribution of hydrogen exchange on apparent N-15 longitudinal relaxation rates in samples with differing D2O buffer content. Differences in the apparent T-1 times allowed us to derive exchange rates for multiple residues in the type III secretion system needle protein. (C) 2017 The Authors. Published by Elsevier Inc.

引用

页码：110 / 116

页数：7

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