Campos-Olivas Ramón, Aziz Rehan, Helms Gregory L, Evans Jeremy N S, Gronenborn Angela M
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Building 5, Room 130, Bethesda, MD 20892, USA.
FEBS Lett. 2002 Apr 24;517(1-3):55-60. doi: 10.1016/s0014-5793(02)02577-2.
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.
通过核磁共振和圆二色光谱对链球菌蛋白G（GB1）的5F-色氨酸取代免疫球蛋白结合结构域B1进行了结构和热力学表征。单个氟报告原子位于三维结构的中心，独特地准备用于研究该蛋白质的内部性质。我们证明，5F-色氨酸的引入不会影响GB1的整体和局部结构，也不会影响其热力学稳定性。氟化GB1的良好特性使其成为开发光谱方法和理论计算的理想模型系统。
