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. 1985 Jul;48(1):9–18. doi: 10.1016/S0006-3495(85)83756-5

Time-resolved x-ray diffraction studies of the sarcoplasmic reticulum membrane during active transport.

J K Blasie, L G Herbette, D Pascolini, V Skita, D H Pierce, A Scarpa
PMCID: PMC1329373  PMID: 3160394

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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