...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Picosecond Dynamics of G-Protein Coupled Receptor Activation in Rhodopsin from Time-Resolved UV Resonance Raman Spectroscopy.
【24h】

Picosecond Dynamics of G-Protein Coupled Receptor Activation in Rhodopsin from Time-Resolved UV Resonance Raman Spectroscopy.

机译：从时间分辨UV共振拉曼光谱从时隙UV共振拉曼光谱法中罗霉素中G蛋白偶联受体激活的皮秒动态。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The protein response to retinal chromophore isomerization in the visual pigment rhodopsin is studied using picosecond time-resolved UV resonance Raman spectroscopy. High signal-to-noise Raman spectra are obtained using a 1 kHz Ti:Sapphire laser apparatus that provides <3 ps visible (466 nm) pump and UV (233 nm) probe pulses. When there is no time delay between the pump and probe events, tryptophan modes W18, W16, and W3 exhibit decreased Raman scattering intensity. At longer pump-probe time delays of +5 and +20 ps, both tryptophan (W18, W16, W3, and W1) and tyrosine (Y1 + 2xY16a, Y7a, Y8a) peak intensities drop by up to 3%. These intensity changes are attributed to decreased hydrophobicity in the microenvironment near at least one tryptophan and one tyrosine residue that likely arise from weakened interaction with the beta-ionone ring of the chromophore following cis-to-trans isomerization. Examination of the crystal structure suggests that W265 and Y268 are responsible for these signals. These UV Raman spectral changes are nearly identical to those observed for the rhodopsin-to-Meta I transition, implying that impulsively driven protein motion by the isomerizing chromophore during the 200 fs primary transition drives key structural changes that lead to protein activation.
机译：使用PICOSECOND时间分辨的UV共振拉曼光谱研究对视觉色素窝中视网膜发色团异构化的蛋白质反应。使用1kHz Ti：Sapphire激光装置获得高信噪比拉曼光谱，其提供<3 PS可见（466nm）泵和UV（233nm）探针脉冲。当泵和探针事件之间没有时间延迟时，色氨酸模式W18，W16和W3表现出降低的拉曼散射强度。在较长的泵探测+ 5和+ 20 ps的时间延迟，色氨酸（W18，W16，W3和W1）和酪氨酸（Y1 + 2xY16a，Y7a，Y8a）峰强度下降至3％。这些强度变化归因于在至少一个色氨酸附近的微环境中减少疏水性，并且一种酪氨酸残基可能因Cis-to-Trans异构化之后的发色团的β-离子环的弱化相互作用而产生。晶体结构的检查表明W265和Y268对这些信号负责。这些UV拉曼光谱变化几乎与观察到的罗经蛋白酶 - 奥基I转化的谱变化相同，这意味着在200 FS初级过渡驱动器期间异构化发色团的冲动驱动的蛋白质运动导致导致蛋白质激活的关键结构变化。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号