CONFORMATIONAL-CHANGES IN PROTEINS PROBED BY HYDROGEN-EXCHANGE ELECTROSPRAY-IONIZATION MASS-SPECTROMETRY

被引：397

作者：

KATTA, V ^{[1
]}

CHAIT, BT ^{[1
]}

机构：

[1] ROCKEFELLER UNIV,NEW YORK,NY 10021

来源：

RAPID COMMUNICATIONS IN MASS SPECTROMETRY | 1991年 / 5卷 / 04期

关键词：

D O I：

10.1002/rcm.1290050415

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Hydrogen-exchange electrospray-ionization mass spectrometry is demonstrated to be an effective new method for probing conformational changes of proteins in solutions. The method is based on the mass spectrometric measurement of the extent of hydrogen/deuterium exchange that occurs in different protein conformers over defined periods of time. Results are presented in which hydrogen-exchange electrospray-ionization mass spectrometry is used to probe conformational changes in bovine ubiquitin induced by the addition of methanol to aqueous acidic solutions of the protein.

引用

页码：214 / 217

页数：4

共 22 条

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