DETERMINATION OF AMIDE HYDROGEN-EXCHANGE RATES IN PEPTIDES BY MASS-SPECTROMETRY

被引：72

作者：

THEVENONEMERIC, G ^{[1
]}

KOZLOWSKI, J ^{[1
]}

ZHANG, ZQ ^{[1
]}

SMITH, DL ^{[1
]}

机构：

[1] PURDUE UNIV,DEPT MED CHEM & PHARMACOGNOSY,W LAFAYETTE,IN 47907

来源：

ANALYTICAL CHEMISTRY | 1992年 / 64卷 / 20期

关键词：

D O I：

10.1021/ac00044a027

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

When proteins are dissolved in D2O, the amide hydrogens are gradually replaced with deuterium. Some amide hydrogens in proteins exchange within seconds, while others resist exchange for months. The rates at which amide hydrogens in proteins undergo isotopic exchange depend on the secondary and tertiary structures of proteins, as well as on experimental variables such as pH and temperature. Because amide hydrogen exchange rates are sensitive to protein structure, they have been used extensively as probes for detecting and understanding conformational changes in proteins. For example, amide hydrogen exchange rates have been used to investigate binding in enzyme/substrate1and antibody/antigen complexes,2to study allosteric changes in hemoglobin,3and to identify intermediates in protein folding. © 1992, American Chemical Society. All rights reserved.

引用

页码：2456 / 2458

页数：3

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