AMIDE HYDROGEN-EXCHANGE AND MASS-SPECTROMETRY - A PROBE OF HIGH-ORDER STRUCTURE IN PROTEINS

被引：13

作者：

SMITH, DL

ZHANG, ZQ

LIU, YQ

机构：

[1] Department of Medicinal Chemistry Purdue University, W. Lafayette IN

来源：

PURE AND APPLIED CHEMISTRY | 1994年 / 66卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1351/pac199466010089

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A new analytical method which facilitates peptide amide hydrogen as a tool for detecting conformational changes and probing high-order structure in large proteins is described. Following a period of deuterium exchange-in, the protein is placed in slow exchange conditions and fragmented into peptides with pepsin. The peptides are analyzed by directly-coupled HPLC fast atom bombardment mass spectrometry to determine their deuterium content. Results presented here demonstrate that this method can be used to determine rate constants for peptide amide hydrogen exchange, and to detect the thermal denaturing of cytochrome c.

引用

页码：89 / 94

页数：6

共 21 条

[1] HYDROGEN-EXCHANGE KINETICS OF BOVINE PANCREATIC TRYPSIN-INHIBITOR BETA-SHEET PROTONS IN TRYPSIN BOVINE PANCREATIC TRYPSIN-INHIBITOR, TRYPSINOGEN BOVINE PANCREATIC TRYPSIN-INHIBITOR, AND TRYPSINOGEN ISOLEUCYLVALINE BOVINE PANCREATIC TRYPSIN-INHIBITOR [J].