A liquid diffraction analysis of sarcoplasmic reticulum. I. Compositional variation

Biophysical Journal
G W BradyG Meissner

Abstract

Intensities of x-ray scattering from a series of fragmented rabbit muscle sarcoplasmic reticulum (SR) samples have been measured over the range x = 0.05 to s = 0.25. By varying the relative concentrations of lipid and protein (chiefly the Mg++-dependent, Ca++- stimulated ATPase) in the membranes of this series, and by employing methods of analysis appropriate to the scattering from binary liquid mixtures, we have identified the separable contributions of protein and lipid, and the protein-lipid interaction contributions to the total scattering profiles. The shape of the protein term is consistent with scattering from a cylindrical ATPase particle 142 A in length and 35 A in diameter. These data imply that the dominant ATPase species is monomeric. The protein-lipid interaction term has been analyzed by a novel treatment based on a determination of the pair correlation function between the electrons of the protein molecule with the electrons of the lipid bilayer in terms of the asymmetry of the transbilayer disposition of the protein. Applied to our results, the analysis indicates a fully asymmetric disposition of ATPase, in which one end of the molecule is contiguous with either the lumenal or cytoplasmic surface of the bilayer.

Citations

Aug 1, 1983·The Journal of Cell Biology·L Castellani, P M Hardwicke
Jan 1, 1984·CRC Critical Reviews in Biochemistry·C Tanford
Jun 1, 1982·Journal of Muscle Research and Cell Motility·P VolpeA Margreth
Jan 17, 1983·European Journal of Biochemistry·H Lüdi, W Hasselbach
Oct 5, 1985·Journal of Molecular Biology·L CastellaniP Vibert
Oct 15, 1984·Biochemical and Biophysical Research Communications·S Highsmith

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