Details of the partial unfolding of T4 lysozyme on quartz using site-directed spin labeling

被引：15

作者：

Jacobsen, Kerstin

Hubbell, Wayne L.

Ernst, Oliver P.

Risse, Thomas

机构：

[1] Fritz Haber Inst Max Planck Soc, Dept Phys Chem, D-14195 Berlin, Germany

[2] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA

[3] Univ Calif Los Angeles, Jules Stein Eye Inst, Los Angeles, CA 90095 USA

[4] Charite Univ Med Berlin, Inst Med Phys & Biophys, D-10098 Berlin, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2006年 / 45卷 / 23期

关键词：

enzymes; EPR spectroscopy; mutagenesis; protein folding; structure elucidation;

D O I：

10.1002/anie.200600008

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) Spin doctoring: Site-directed spin labeling was used to determine the structure of T4 lysozyme adsorbed on quartz. At high ionic strength significant changes of the backbone fold are limited to the region around the enzymatic cleft. In contrast, at low ionic strength the previously unperturbed parts of the protein interact with the surface. Hydrophobic interactions are thought to play an important role in the partial unfolding at high ionic strength. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：3874 / 3877

页数：4

共 46 条

[1] Xenogeneic extracellular matrix as a scaffold for tissue reconstruction [J].