Inhaltszusammenfassung

ATP-synthase, a membrane protein of the biological energy metabolism, has been investigated in the solution of a non-denaturating detergent (taurodeoxycholate) and bound to lipid membranes. The aggregation of the detergent solubilized enzyme was avoided by reconstitution into small unilamellar lipid vesicles as simplified cell membrane models. The structure of the protein in situ, i.e. reconstituted to liposomes of DMPC-D54, was investigated by neutron small angle scattering. The scattering o...ATP-synthase, a membrane protein of the biological energy metabolism, has been investigated in the solution of a non-denaturating detergent (taurodeoxycholate) and bound to lipid membranes. The aggregation of the detergent solubilized enzyme was avoided by reconstitution into small unilamellar lipid vesicles as simplified cell membrane models. The structure of the protein in situ, i.e. reconstituted to liposomes of DMPC-D54, was investigated by neutron small angle scattering. The scattering of the lipid entity was masked by solvent contrast matching using a D2O-buffer containing 86% heavy water and 10% glycerol, 5 mM TDOC. The structure of the membrane bound enzyme resembled that of the detergent solubilized protein.» weiterlesen» einklappen

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Klassifikation

DDC Sachgruppe:
Biowissenschaften, Biologie