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  • 1
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 2 (1974), S. 538-557 
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Alamethicin, monazomycin, or EIM induce electrical excitability in lipid bilayers. The voltage-dependent gating displays all the characteristics observed in excitable cells and its basic features can be quantitatively described by the Hodgkin-Huxley equations.A common molecular mechanism of membrane excitation has been postulated. It assumes that in the absence of an electrical field the channel-forming molecules lie at the surface of the membrane. An applied potential tilts them from the surface into the hydrocarbon region of the bilayer. Once in this position the molecules diffuse laterally and form aggregates which act as channels for the flow of ions.In the case of alamethicin we assume that the molecule forms an elongated ellipsoid with two glutamic residues at one end, and a metal ion in four- or five-fold coordination with peptide carbonyl oxygens at the other. An applied field pulls the cationic end through the membrane to the other side, while the glutamic residues hold the other end attached to the original surface. The molecules now span the membrane and aggregate, forming oligomeric channels in which most of the peptide carbonyls face toward the center, and the methyl groups outward.Monomers and dimers do not conduct and an individual channel can have different conductance values depending on the number of monomers in the aggregate and the resulting channel diameter. A quantitative description of this process matches observed gating kinetics, gating currents, and the single channel conductance increments. Without additional assumptions, inactivation follows directly from the aggregation process because with proper rate constants, the average degree of polymerization and therefore number of open channels goes through a maximum in time.The model may also apply to the excitation process of higher cells.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 1 (1972), S. 60-65 
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: As a first step in the study of chorion composition, biochemical development and morphogenesis, we have studied the proteins of moth chorions (eggshells). We draw attention to the extensive similarities of these proteins in a variety of species. We also report that the eggshell proteins are deposited in succession, each with its characteristic time table. This phenomenon may be related to the morphogenesis of chorion.
    Additional Material: 2 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 2 (1974), S. 108-120 
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 2 (1974), S. 166-177 
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The assembly of E. coli ribosomes has been studied through the analysis of a new group of ribosome maturation mutants. These mutants, all blocked in a late stage in the maturation of 50S ribosomes, map at four different sites on the chromosome. These sites are distant from the known ribosomal protein sites at the str-aro E region of the chromosome. The ribosome precursor particles of the mutants contain precursor-type 23S RNA (p23 RNA) and 5S RNA. 43S particles of one of the mutants contain all but one of the normal complement of proteins. Precursor 43S particles from this mutant can be converted to particles with sedimentation values around 50S by incubation with extracts from either the wild-type organism or from other mutants. This in vitro conversion process differs considerably from the process of ribosome reconstitution and indicates a role for extrinsic factors in the maturation of E. coli ribosomes.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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