Placement of 19F into the center of GB1:: effects on structure and stability
Placement of 19F into the center of GB1:: effects on structure and stability
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DOI：
10.1016/s0014-5793(02)02577-2
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发表时间：
2002-04-24
期刊：
影响因子：
3.5
通讯作者：
Gronenborn, AM
中科院分区：
文献类型：
--
作者：
Campos-Olivas, R;Aziz, R;Gronenborn, AM
用核磁共振和圆二色性光谱对链球菌G蛋白（GB 1）的免疫球蛋白结合区B1进行了结构和热力学表征。一个单一的氟报告原子位于三维结构的中心，独特地准备用于研究这种蛋白质的内部性质。我们证明了5 F-Trp的引入不影响GB 1的全局和局部结构，并且对热力学稳定性没有影响。氟化的GB 1的有利性质使该分子成为发展光谱方法和理论计算的理想模型系统。(C)2002年欧洲生物化学学会联合会。由Elsevier Science B. V.出版，版权所有。
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.