Oxidative phosphorylation and proton translocation in membrane vesicles prepared from Escherichia coli |
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Authors: | E L Hertzberg P C Hinkle |
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Affiliation: | 1. Department of Chemistry, University of South Florida, Tampa, Florida 33620, USA;2. Max-Planck-Institut für Molekulare Genetik, Abt. Wittmann, Berlin-Dahlem, Germany |
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Abstract: | This paper reports physical-chemical properties of proteins L7 and L12 from E. coli 50 S subunits. Evidence is presented that these two proteins behave in their native state as a dimer of molecular weight 24000. From sedimentation velocity and intrinsic viscosity data the actual frictional ratio of the dimer has been obtained revealing an asymmetric particle which can be described as a rod with cell dimensions of L = 130 Å and a diameter of D = 17.0 Å. From small X-ray scattering the radius of gyration (Rg = 37.0 Å), the thickness factor, and the degree of hydration were determined. This indicates that the extended shape of the dimer is due to the asymmetry of the molecule and not to the hydration. |
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Keywords: | All correspondence please to present address: Institut für Pflanzenphysiologie und Zellbiologie Abt. Biochemie D-1000 Berlin 33 Königin-Luise-Str. 1216a Germany. |
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