Dynamics of Biomolecules in Photoreceptor Cells of Twilight and Color Vision

我们的项目已经完成了。[1]共振拉曼光谱学研究在7，9-dicis-rhodopsin中演示了在其色素（7，9-dicis-retinal）之间的Schiff基础连接和bovine opsin保留了作为rhodopsin的情况下。[2]在Lumi-meta I过渡期间，rhodopsin和7-顺式rhodopsin之间的照片比较揭示了opsin和9-甲基组的色素发生了变化。[3]对合成rhodopsin模拟的照片的分析表明，一个围绕Beta的修饰性变化-变色龙的离子环应该在Batho-Lumi过渡期间使用。[4]激光闪光灯的8-成员-rhodopsin显示了照片-batho过渡过程的相关路径，是反式C_<11>-C_<12>双键高度扭曲的形成在色谱中的一个轻松的路径。[5]FTIR光谱仪显示了Schiff基的Hypsorhodopsin是被保护的。[6]在细菌霍多普辛的光周期中，一种增加 ... More f蛋白质活力和视网膜色素的原始Schiff基础之间的相互作用，通过FTIR光谱学观察到了L和N中间物的阶段。[7]FTIR光谱显示，在N介导的Asp-96中，在Asp-85被抑制的情况下，细菌性多普勒被抑制。[8]Chromophore提取实验表明，iodopsin的光致发光是由视网膜色素中C_<11>-C_<12>双键的顺式反式异构化启动的。[9]有人建议说，甲odopsin II的生命周期将比甲odopsin II的寿命短得多。[10]对我们的单克隆抗体特性的外itope（s）的分析（s）现已被调查。“碘多普辛的C-终端部分可能是抗原性物质。”[11]一种光致性的介质iodopsin被磷酸化了，被纯化的bovine rhodopsin激酶。[12]一种可选蛋白质-特异性G蛋白α-子单元部分由鸡视网膜素纯化。[13]iodopsin的氨基酸序列是从其补充DNA中提取的。在一只鸡视网膜上克隆其他圆锥形颜料现在正在进行中。Less（低）

Following progresses have been made. [1] Resonance Raman spectroscopic study on 7, 9-dicis-rhodopsin demonstrated that the Schiff base linkage between its chromophore (7, 9-dicis-retinal) and bovine opsin retained anti form as in the case of rhodopsin. [2] A comparison of photoreactions between rhodopsin and 7-cis-rhodopsin revealed that an interaction between opsin and the 9-methylgroup of the chromophore changed during the lumiーmeta I transition. [3] Analysis of the photoreactions of synthetic rhodopsin analogs indicated that a conformational change around betaーionone ring of the chromophore should occur during bathoーlumi transition. [4] Laser flash photolysis of 8-memberedーrhodopsin showed that photoーbatho transition process corresponded to a relaxing pathway of highly twisted conformation of trans C_<11>-C_<12> double bond in the chromophore. [5] FTIR spectroscopy showed that the Schiff base of hypsorhodopsin was protonated. [6] In the photocycle of bacteriorhodopsin, an increase o … More f interaction between the protein moiety and the protonated Schiff base of the retinylidene chromophore was observed at the stages of both L and N intermediates by FTIR spectroscopy. [7] FTIR spectroscopy showed that Asp-96 in N intermediated of bacteriorhodopsin was deprotonated while Asp-85 was protonated. [8] Chromophore extraction experiments indicated that the photobleaching of iodopsin was initiated by the cis-trans isomerization of C_<11>-C_<12> double bond in the retinylidene chromophore. [9] It was suggested that the lifetime of metaiodopsin II would be extremely shorter than that of metarhodopsin II. [10] Analysis of epitope (s) of our monoclonal antibodies specific for iodopsin is now being investigated. The C-terminal part of iodopsin could be the antigenic ite. [11] A photobleaching intermediate of iodopsin was phosphorylated by purified bovine rhodopsin kinase. [12] A candidate protein for putative cone-specific G-protein alpha-subunit was partially purified from chicken retinas. [13] Amino acid sequence of iodopsin was deduced from its complementary DNA. Cloning of the other cone pigments in a chicken retina is now under progress. Less