MODIFIED TRIPLE-RESONANCE NMR EXPERIMENTS WITH OPTIMIZED SENSITIVITY FOR RAPIDLY EXCHANGING PROTONS

被引：6

作者：

JAHNKE, W ^{[1
]}

KESSLER, H ^{[1
]}

机构：

[1] TECH UNIV MUNICH,INST ORGAN CHEM & BIOCHEM,D-85747 GARCHING,GERMANY

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION IN ENGLISH | 1995年 / 34卷 / 04期

关键词：

NMR SPECTROSCOPY; STRUCTURE ELUCIDATION; PROTEINS;

D O I：

10.1002/anie.199504691

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Fast exchange with surrounding water protons need not attenuate 1H NMR signals of proteins in solution. A modified pulse sequence has been developed to increase the signal intensity of the amide protons; on the right the improvement in sensitivity (a → c) is shown for a selected residue in a protein. This new technique should aid elucidation of protein structures in solution. (Figure Presented.) Copyright © 1995 by VCH Verlagsgesellschaft mbH, Germany

引用

页码：469 / 471

页数：3