Effects of Membrane Thickness on the Molecular Dynamics and Enzymic Activity of Reconstituted Ca-ATPase
- 15 March 1994
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 33 (10) , 2912-2920
- https://doi.org/10.1021/bi00176a022
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 34 references indexed in Scilit:
- The effect of bilayer thickness and n-alkanes on the activity of the (Ca2+ + Mg2+)-dependent ATPase of sarcoplasmic reticulum.Journal of Biological Chemistry, 1981
- Highly purified sarcoplasmic reticulum vesicles are devoid of Ca2+-independent (‘basal’) ATPase activityBiochimica et Biophysica Acta (BBA) - Biomembranes, 1980
- Effect of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranesBiophysical Journal, 1980
- Enzyme kinetics and substrate stabilization of detergent-solubilized and membraneous (Ca2+ + Mg2+)-activated ATPase from sarcoplasmic reticulum. Effect of protein-protein interactions.Journal of Biological Chemistry, 1980
- Theory of protein-lipid and protein-protein interactions in bilayer membranes.Proceedings of the National Academy of Sciences, 1979
- Protein-lipid interactions in bilayer membranes: A lattice modelProceedings of the National Academy of Sciences, 1979
- Rotational motion of the sarcoplasmic reticulum Ca2+-ATPase.Proceedings of the National Academy of Sciences, 1978
- Effect of the lipid environment on protein motion and enzymatic activity of sarcoplasmic reticulum calcium ATPase.Journal of Biological Chemistry, 1978
- Theoretical study of protein--lipid interactions in bilayer membranes.Proceedings of the National Academy of Sciences, 1978
- DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTIONJournal of Biological Chemistry, 1949