Conformational flexibility of avidin: the influence of biotin binding

被引：15

作者：

Celej, MS ^{[1
]}

Montich, GG ^{[1
]}

Fidelio, GD ^{[1
]}

机构：

[1] Univ Nacl Cordoba, CIQUIBIC, Dept Quim Biol, Fac Ciencias Quim, RA-5000 Cordoba, Argentina

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 325卷 / 03期

关键词：

protein stability; ligand binding; conformational flexibility; FTIR; H/D exchange; avidin; biotin;

D O I：

10.1016/j.bbrc.2004.10.118

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：

Ligand binding to proteins is a key process in cell biochemistry. The interaction usually induces modifications in the unfolding thermodynamic parameters of the macromolecule due to the coupling of unfolding and binding equilibria. In addition, these modifications can be attended by changes in protein structure and/or conformational flexibility induced by ligand binding. In this work, we have explored the effect of biotin binding on conformation and dynamic properties of avidin by using infrared spectroscopy including kinetics of hydrogen/deuterium exchange. Our results, along with previously thermodynamic published data, indicate a clear correlation between thermostability and protein compactness. In addition, our results also help to interpret the thermodynamic binding parameters of the exceptionally stable biotin:AVD complex. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：922 / 927

页数：6

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