By Lyle V. Beck, Malcolm Dixon, W. Eugene Knox (auth.), Sidney Fleischer, Youssef Hatefi, David H. MacLennan, Alexander Tzagoloff (eds.)
On February 14, 1977, a symposium entitled "The Molecular Biology of Membranes" was once held in New Orleans in honor of Professor David E. eco-friendly, whose many contributions in mitochondrial constitution and metabolism have stimulated and guided examine during this very important sector of biochemistry for a few years. The symposium used to be attended via many former and present-day colleagues, pals, and scientists. The contents of this quantity signify papers that have been brought on the symposium and different contributions from people who were affiliates of Professor eco-friendly. we want to thank Plenum Press for his or her help make the symposium and book of this e-book attainable. Sidney Fleischer Youssef Hatefi David MacLennan Alexander Tzagoloff vii Contents Impressions of David E. eco-friendly through His Colleagues . . . . . . . . . . . . . . 1 Enzyme Institute Days thirteen F. M. Huennekens point of view for the Mitochondrion 17 David E. eco-friendly bankruptcy 1 association of Protein and Lipid elements in Membranes 29 Garret Vanderkooz bankruptcy 2 constitution of the Mitochondrion . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . fifty seven Robert A. Haworth and Douglas R. Hunter bankruptcy three Permeability of Membrane as an element picking out the speed of Mitochondrial respiratory: position of Ultrastructure . . . . . . . . . . . . . . seventy five Jerzy Popinigis bankruptcy four Chemistry of Intrinsic Membrane Protein Complexes: stories on complicated III and Cytochrome c Oxidase . . . . . . . . . . . . . . . . . . . . . . . 103 Roderick A. Capaldi ix x Contents bankruptcy five Reversible Mitochondrial ATPase as a version for the answer of a 121 Membrane complicated A. E.
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Additional resources for The Molecular Biology of Membranes
The nonbonded energy of interaction between entire protein molecules has not been given much consideration, however, since for proteins in aqueous solution these forces are ordinarily overshadowed by the electrostatic forces. In the course of seeking to identify the various types of intermolecular interactions that may exist between proteins which are partially immersed in the hydrophobic portion of a lipid bilayer, we carried out some fairly crude calculations in order to see if the nonbonded interactions may in fact be of a significant magnitude.
The sphere and cube geometries are self-explanatory. Parallel, juxtaposed faces of the pair of interacting cubes were assumed. Square plates having a constant thickness of 50 Awere also studied, with the size of the square faces varying according to the molecular weight. The juxtaposed sides of the pair of plates were kept parallel to each other. Several points are worthy of note. First, the nonbonded energy between proteins embedded in lipid is necessarily attractive; this statement is true independent of the particular parameters or geometries employed.
The ability of the proteins in a membrane to move by no means implies that their distribution in the plane of the membrane will be random, however. Freeze-fracture electron microscopy has demonstrated that change of pH or temperature can cause changes in the state of distribution of the intrinsic membrane proteins in several membranes, including erythrocytes, (10) recombined rhodopsin membranes, (11) and mitochondria, (12) among others. (13,14) In these cases, nonphysiological conditions were employed to induce a gross change from a state in which the proteins are fairly randomly scattered throughout the available membrane area to one in which they have become aggregated into clusters, leaving large areas of protein-free lipid bilayer.
The Molecular Biology of Membranes by Lyle V. Beck, Malcolm Dixon, W. Eugene Knox (auth.), Sidney Fleischer, Youssef Hatefi, David H. MacLennan, Alexander Tzagoloff (eds.)