A Fourier transform infrared spectroscopic study of yeast hexokinase: conformational changes under interaction with substrates and inhibitors

被引：5

作者：

Trinquier-Dinet, M

Boisdon, MT

Perie, J

Willson, M ^{[1
]}

机构：

[1] Univ Toulouse 3, Serv Commun Spect Infrarouge, F-31062 Toulouse, France

[2] Univ Toulouse 3, CNRS, UMR 5623, Grp Chim Organ Biol, F-31062 Toulouse, France

来源：

SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY | 1998年 / 54卷 / 02期

关键词：

hexokinase; FTIR; inhibitors; conformational changes; hydrated structure;

D O I：

10.1016/S1386-1425(98)00005-5

中图分类号：

O433 [光谱学];

学科分类号：

0703 ; 070302 ;

摘要：

The infrared (FTIR) spectroscopy study of several complexes of yeast hexokinase with substrates and inhibitors allows the determination of open and closed conformations of the protein. The analysis is based on a correlation between FTIR and X-ray data for one of the inhibitor-enzyme complexes of the study and from that reference, the features of the amide I band hydration component. (C) 1998 Elsevier Science B.V.

引用

页码：367 / 373

页数：7

共 23 条

[11] COMPARISON OF VARIOUS MOLECULAR-FORMS OF BOVINE TRYPSIN - CORRELATION OF INFRARED-SPECTRA WITH X-RAY CRYSTAL-STRUCTURES [J].