Bacteriorhodopsin molecular dynamics: photobleaching and chemical cross-linking

Proceedings of 16th Annual International Conference of the IEEE Engineering in Medicine and Biology Society Pub Date : 1994-11-03 DOI:10.1109/IEMBS.1994.415269

J. Draheim, J. Cassim

{"title":"Bacteriorhodopsin molecular dynamics: photobleaching and chemical cross-linking","authors":"J. Draheim, J. Cassim","doi":"10.1109/IEMBS.1994.415269","DOIUrl":null,"url":null,"abstract":"The conformational capabilities of the in situ transmembrane protein bacteriorhodopsin (bR) were studied by mid-IR linear dichroism of purple membrane (PM) films. Illumination of bR, with a Schiff-base bound retinylidene prosthetic group, is usually accompanied by the vectorial translocation of H/sup +/ across the membrane bilayer. In the presence of hydroxylamine HCl however, illumination hydrolyzes the Schiff-base linkage between bR and its retinylidene chromophore (photobleaching). Analysis of the mid-IR linear dichroism of PM indicates: (1) the /spl alpha/-helical segments in bR are oriented nearly parallel to the PM normal; (2) after photobleaching the PM, the /spl alpha/-helical segments of bR are tilted 24/spl deg/ away from the PM normal; (3) after cross-linking PM with dimethyl adipimidate the /spl alpha/-helical segments of bR are tilted 9/spl deg/ away from the PM normal; (4) after cross-linking and photobleaching, the /spl alpha/-helical segments of bR are tilted 30/spl deg/ away from the PM normal.<<ETX>>","PeriodicalId":344622,"journal":{"name":"Proceedings of 16th Annual International Conference of the IEEE Engineering in Medicine and Biology Society","volume":"21 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"1994-11-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Proceedings of 16th Annual International Conference of the IEEE Engineering in Medicine and Biology Society","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1109/IEMBS.1994.415269","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}

引用次数: 0

Abstract

The conformational capabilities of the in situ transmembrane protein bacteriorhodopsin (bR) were studied by mid-IR linear dichroism of purple membrane (PM) films. Illumination of bR, with a Schiff-base bound retinylidene prosthetic group, is usually accompanied by the vectorial translocation of H/sup +/ across the membrane bilayer. In the presence of hydroxylamine HCl however, illumination hydrolyzes the Schiff-base linkage between bR and its retinylidene chromophore (photobleaching). Analysis of the mid-IR linear dichroism of PM indicates: (1) the /spl alpha/-helical segments in bR are oriented nearly parallel to the PM normal; (2) after photobleaching the PM, the /spl alpha/-helical segments of bR are tilted 24/spl deg/ away from the PM normal; (3) after cross-linking PM with dimethyl adipimidate the /spl alpha/-helical segments of bR are tilted 9/spl deg/ away from the PM normal; (4) after cross-linking and photobleaching, the /spl alpha/-helical segments of bR are tilted 30/spl deg/ away from the PM normal.<>

查看原文本刊更多论文

细菌视紫红质分子动力学:光漂白和化学交联

利用紫膜(PM)薄膜的中红外线性二色性研究了原位跨膜蛋白细菌紫紫红质(bR)的构象能力。用希夫碱结合视黄嘌呤假基照射bR，通常伴随着H/sup +/跨膜双分子层的载体移位。然而，在羟胺HCl存在下，光照水解bR与其视黄醛发色团之间的希夫碱键(光漂白)。PM的中红外线性二色性分析表明:(1)bR中的/spl α /-螺旋段取向与PM法线接近平行;(2)光漂白PM后，bR的/spl α /-螺旋段向PM法向倾斜24/spl度;(3) PM与己烯二甲酯交联后，bR的/spl α /-螺旋段向PM法向倾斜9/spl度;(4)经交联和光漂白后，bR的/spl α /-螺旋段向PM法向倾斜30/spl度。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Proceedings of 16th Annual International Conference of the IEEE Engineering in Medicine and Biology Society

自引率

0.00%

发文量