SPECTRAL METHODS FOR STUDY OF THE G-PROTEIN-COUPLED RECEPTOR RHODOPSIN. I. VIBRATIONAL AND ELECTRONIC SPECTROSCOPY.
SPECTRAL METHODS FOR STUDY OF THE G-PROTEIN-COUPLED RECEPTOR RHODOPSIN. I. VIBRATIONAL AND ELECTRONIC SPECTROSCOPY.
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研究 G 蛋白偶联受体视紫红质的光谱方法。
DOI：
10.1134/s0030400x15050240
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发表时间：
2015
影响因子：
0.6
通讯作者：
Brown,MF
中科院分区：
文献类型：
--
作者：
Struts,AV;Barmasov,AV;Brown,MF
在这里，我们回顾了现代光谱方法在以视紫红质为原型的G蛋白偶联受体(GPCRs)研究中的应用。由于X射线分析给我们提供了蛋白质构象的固定快照，因此必须应用光谱方法来阐明它们的功能：振动(拉曼，FTIR)光谱，电子(紫外可见吸收，荧光)光谱，磁共振(电子顺磁共振，EPR)和核磁共振(核磁共振)。在这两篇文章的第一篇中，我们讨论了光学光谱学在膜环境中研究视紫红质的应用。获得关于视紫红质激活中事件的时间顺序的信息。发色团的异构化和视网膜Schiff碱的去质子化导致蛋白质的结构变化，涉及到H5和H6螺旋的运动，这是一个pH依赖的过程。获得了从X射线结晶学中无法获得的信息，这可以与光谱学研究相结合，以实现对GPCR功能的更全面的了解。
Here we review the application of modern spectral methods for the study of G-protein-coupled receptors (GPCRs) using rhodopsin as a prototype. Because X-ray analysis gives us immobile snapshots of protein conformations, it is imperative to apply spectroscopic methods for elucidating their function: vibrational (Raman, FTIR), electronic (UV-visible absorption, fluorescence) spectroscopies, and magnetic resonance (electron paramagnetic resonance, EPR), and nuclear magnetic resonance (NMR). In the first of the two companion articles, we discuss the application of optical spectroscopy for studying rhodopsin in a membrane environment. Information is obtained regarding the time-ordered sequence of events in rhodopsin activation. Isomerization of the chromophore and deprotonation of the retinal Schiff base leads to a structural change of the protein involving the motion of helices H5 and H6 in a pH-dependent process. Information is obtained that is unavailable from X-ray crystallography, which can be combined with spectroscopic studies to achieve a more complete understanding of GPCR function.