期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 56, 期 22, 页码 6122-6125出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201610759
关键词
amide protons; conformational dynamics; cross relaxation; proteins; proton CEST
资金
- Canadian Institutes of Health Research
An amide H-1-Chemical Exchange Saturation Transfer (CEST) experiment is presented for studies of conformational exchange in proteins. The approach, exploiting spin-state-selective magnetization transfer, completely suppresses undesired NOE-based dips in CEST profiles so that chemical exchange processes can be studied. The methodology is demonstrated with applications involving proteins that interconvert on the millisecond timescale between major and invisible minor states, and accurate amide H-1 chemical shifts of the minor conformer are obtained in each case. The spin-state-selective magnetization transfer approach offers unique possibilities for quantitative studies of protein exchange through H-1-CEST.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据