Time-resolved x-ray diffraction studies of the sarcoplasmic reticulum membrane during active transport.
作者信息
Blasie J K, Herbette L G, Pascolini D, Skita V, Pierce D H, Scarpa A
出版信息
Biophys J. 1985 Jul;48(1):9-18. doi: 10.1016/S0006-3495(85)83756-5.
Abstract
X-ray and neutron diffraction studies of oriented multilayers of a highly purified fraction of isolated sarcoplasmic reticulum (SR) have previously provided the separate profile structures of the lipid bilayer and the Ca2+-ATPase molecule within the membrane profile to approximately 10-A resolution. These studies used biosynthetically deuterated SR phospholipids incorporated isomorphously into the isolated SR membranes via phospholipid transfer proteins. Time-resolved x-ray diffraction studies of these oriented SR membrane multilayers have detected significant changes in the membrane profile structure associated with phosphorylation of the Ca2+-ATPase within a single turnover of the Ca2+-transport cycle. These studies used the flash photolysis of caged ATP to effectively synchronize the ensemble of Ca2+-ATPase molecules in the multilayer, synchrotron x-radiation to provide 100-500-ms data collection times, and double-beam spectrophotometry to monitor the Ca2+-transport process directly in the oriented SR membrane multilayer.
摘要
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Static and time-resolved structural studies of the Ca2+-ATPase of isolated sarcoplasmic reticulum.分离的肌浆网Ca2+ -ATP酶的静态和时间分辨结构研究。
Ann N Y Acad Sci. 1982;402:478-84. doi: 10.1111/j.1749-6632.1982.tb25770.x.
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