Substrate binding and enzyme function investigated by infrared spectroscopy

被引:42
作者
Barth, A [1 ]
Zscherp, C [1 ]
机构
[1] Goethe Univ Frankfurt, Inst Biophys, D-60590 Frankfurt, Germany
来源
FEBS LETTERS | 2000年 / 477卷 / 03期
关键词
ATPase; kinase; H-Ras P21; GroEL; Fourier transform infrared spectroscopy; nucleotide;
D O I
10.1016/S0014-5793(00)01782-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein conformational changes triggered by molecule binding are increasingly investigated by infrared spectroscopy often using caged compounds, Several examples of molecule-protein recognition studies are given, which focus on nucleotide binding to proteins. The investigation of enzyme mechanisms is illustrated in detail using the Ca2+-ATPase of the sarcoplasmic reticulum membrane as an example. It is shown that infrared spectroscopy provides valuable information on general aspects of enzyme function as well as on molecular details of molecule-protein interactions and the mechanism of catalysis, (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
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页码:151 / 156
页数:6
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