help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

Biophysical Journal 48: 9-18 (1985)
© 1985 the Biophysical Society

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Blasie, J K
Right arrow Articles by Scarpa, A
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Blasie, J K
Right arrow Articles by Scarpa, A

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 and A Scarpa

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.




This article has been cited by other articles:


Home page
 Biophys. JHome page
I. Y. Churbanova, A. Tronin, J. Strzalka, T. Gog, I. Kuzmenko, J. S. Johansson, and J. K. Blasie
Monolayers of a Model Anesthetic-Binding Membrane Protein: Formation, Characterization, and Halothane-Binding Affinity
Biophys. J., May 1, 2006; 90(9): 3255 - 3266.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. H. MacLennan, W. J. Rice, and N. M. Green
The Mechanism of Ca2+ Transport by Sarco(Endo)plasmic Reticulum Ca2+-ATPases
J. Biol. Chem., November 14, 1997; 272(46): 28815 - 28818.
[Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Barth, F. von Germar, W. Kreutz, and W. Mantele
Time-resolved Infrared Spectroscopy of the Ca2+-ATPase. THE ENZYME AT WORK
J. Biol. Chem., November 29, 1996; 271(48): 30637 - 30646.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
S. Gruner
Time-resolved x-ray diffraction of biological materials
Science, October 16, 1987; 238(4825): 305 - 312.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1985 by the Biophysical Society.