Placement of 19F into the center of GB1:: effects on structure and stability

被引：46

作者：

Campos-Olivas, R

Aziz, R

Helms, GL

Evans, JNS

Gronenborn, AM

机构：

[1] NIDDKD, Chem Phys Lab, NIH, Bethesda, MD 20892 USA

[2] Washington State Univ, Ctr NMR Spect, Pullman, WA 99164 USA

[3] Washington State Univ, Sch Mol Biosci, Pullman, WA 99164 USA

来源：

FEBS LETTERS | 2002年 / 517卷 / 1-3期

关键词：

immunoglobulin G binding domain B1 of; streptococcal protein G; fluorine substitution; protein structure; nuclear magnetic resonance;

D O I：

10.1016/S0014-5793(02)02577-2

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：

A structural and thermodynamic characterization of 5F-Trp-substituted immunoglobulin binding domain B1 of streptococcal protein G (GB1) was carried out by nuclear magnetic resonance and circular dichroism spectroscopy. A single fluorine reporter atom was positioned at the center of the three-dimensional structure, uniquely poised to be exploited for studying interior properties of this protein. We demonstrate that the introduction of 5F-Trp does not affect the global and local architecture of GB1 and has no influence on the thermodynamic stability. The favorable properties of the fluorinated GB1 render this molecule a desirable model system for the development of spectroscopic methodology and theoretical calculations. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：55 / 60

页数：6

共 14 条

[1] THERMODYNAMIC ANALYSIS OF THE FOLDING OF THE STREPTOCOCCAL PROTEIN-G IGG-BINDING DOMAINS B1 AND B2 - WHY SMALL PROTEINS TEND TO HAVE HIGH DENATURATION TEMPERATURES [J].