Functional dynamics of a LOV domain based photoactivated adenylate cyclase revealed by time-resolved small/wide angle X-ray scattering
收藏ESRF Portal2028-01-01 更新2026-04-23 收录
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https://doi.esrf.fr/10.15151/ESRF-ES-2227848985
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资源简介:
Optogenetics is an emerging field of scientific research where genetically encoded photoreceptor proteins are used in order to perform cellular, intermolecular tasks. Photoreceptor proteins are now used as optogenetical devices to control heterodimerization, homodimerization, gene expression, degradation, nuclear-cytosolic translocation, or the cytoskeleton's function. The most favorable light-activated proteins for the optogenetic toolbox are flavin (FAD or FMN) based photoreceptors like BLUF domain, LOV domain proteins or cryptochromes. We propose to use time-resolved X-ray solution scattering (TR-XSS) experiments to study the functional dynamics of two LOV domain proteins – El222 and mPAC – which can serve as optimal optogenetic devices. The TR-XSS measurements will elucidate the steps of the structural changes after photoexcitation in both proteins, which will helps us to engineer better optogenetic proteins.
提供机构:
UNIVERSITY OF PECS, DEPARTMENT OF BIOPHYSICS, Szigeti street 12., 7624 Pecs, Hungary; Institut de Biologie Structurale - IBS, 71 avenue des Martyrs, CS 10090, 38044 Grenoble Cedex 9, France; University of Pecs, Department of Biophysics, Szigeti ut 12, 7624 Pecs, Hungary; Institut de Biologie Structurale - IBS, 71 avenue des Martyrs CS 10090, 38044, Grenoble, FRANCE; UNIVERSITY OF PECS, DEPARTMENT OF BIOPHYSICS, Szigeti street 12., 7624, Pecs, HUNGARY; CNRS, UMR 9198, I2BC, 1 avenue de la Terrasse, 91198, Gif-sur-yvette, FRANCE
创建时间:
2028-01-01



