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  • 1
    Digitale Medien
    Digitale Medien
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 96 (1992), S. 10019-10025 
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    The journal of membrane biology 119 (1991), S. 109-132 
    ISSN: 1432-1424
    Schlagwort(e): channels ; energy profiles ; molecular dynamics ; molecular mechanics ; structure ; function ; icosahedral viruses ; acetylcholine receptor channel ; gramicidin ; ion permeation ; ion selectivity
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Springer
    The journal of membrane biology 119 (1991), S. 141-149 
    ISSN: 1432-1424
    Schlagwort(e): iron uptake ; transferrin ; endocytosis ; reticulocytes ; iron mobilization ; iron translocation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Summary The kinetics of the separate processes of Fe2(III)-transferrin binding to the transferrin receptor, transferrin-receptor internalization, iron dissociation from transferrin, iron passage through the membrane, and iron mobilization into the cytoplasm were studied by pulse-chase experiments using rabbit reticulocytes and59Fe,125I-labeled rabbit transferrin. The binding of59Fe-transferrin to transferrin receptors was rapid with an apparent rate constant of 2×105 m −1 sec−1. The rate of internalization of59Fe-transferrin was directly measured at 520±100 molecules of Fe2(III)-transferrin internalized/sec/cell with 250±43 sec needed to internalize the entire complement of reticulocyte transferrin receptors. Subsequent to Fe2(III)-transferrin internalization the flux of59Fe was followed through three compartments: internalized transferrin, membrane, and cytosol. A process preceding iron dissociation from transferrin and a reaction involving membrane-associated iron required 17±2 sec and 34±5 sec, respectively. Apparent rate constants of 0.0075±0.002 sec−1 and 0.0343±0.0118 sec−1 were obtained for iron dissociation from transferrin and iron mobilization into the cytosol, respectively. Iron dissociation from transferrin is the rate-limiting step. An apparent rate constant of 0.0112±0.0025 sec−1 was obtained for processes involving iron transport through the membrane although at least two reactions are likely to be involved. Based on mechanistic considerations, iron transport through the membrane may be attributed to an iron reduction step followed by a translocation step. These data indicate that the uptake of iron in reticulocytes is a sequential process, with steps after the internalization of Fe2(III)-transferrin that are distinct from the handling of transferrin.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Springer
    The journal of membrane biology 30 (1976), S. 197-212 
    ISSN: 1432-1424
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Summary The permeability of isolated muscle fibers of the giant barnacleMegabalanus psittacus to water and nonelectrolytes was studied by determining their reflection and permeability coefficients. Reflection coefficients were obtained by comparing the osmotic fluxes produced by a test molecule to that produced by the impermeant sucrose molecule. Permeability coefficients were determined for measurements of tracer uptake. The results indicate that, in these fibers, nonelectrolyte permeability is closely related to lipid solubility and molecular size. A value of 2.16×10−12 cm3/sec dyne for the hydraulic conductivity and a value of 10.45×10−4 cm/sec for3HHO permeability coefficient were obtained. The effect of membrane surface invaginations and clefts on the determination of permeability coefficients is discussed.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 5
    Digitale Medien
    Digitale Medien
    Springer
    The journal of membrane biology 91 (1986), S. 11-18 
    ISSN: 1432-1424
    Schlagwort(e): smooth muscle ; Ca-activated K channel ; conduction ; selectivity ; bilayers
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Summary Interaction of vesicles from a microsomal fraction of rabbit intestinal smooth muscle with planar bilayers promotes the incorporation of a large conductance potassium-selective channel. The channel conductance fluctuates between two states: closed and open and the fraction of time the channel dwells in the open state is a function of the electric potential difference and the calcium concentrations. This channel seems to correspond to a Ca-activated K channel described by other authors in smooth muscle cells with the patch-clamp technique. Single-channel conductance is a saturating function of the potassium concentration. The relationship between conductance and concentration cannot be described by a hyperbolic function, suggesting multiple occupancy of the channel. The single-channel conductance is 230 pS in symmetrical 0.1m KCl. Current is a linear function of the applied voltage in the range between −100 and +100 mV, at concentrations of 0.1m KCl or higher. At lower concentrations, current-to-voltage curves bend symmetrically to the voltage axis. Sodium, lithium and cesium ions do not pass through the channel and the permeability for Rb is 66% that of potassium. All these alkali cations and Ca2+ block the channel in a voltage-dependent manner. A two-site three-barrier model on Eyring absolute reaction rate theory can account for the conduction and blocking characteristics.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 6
    Digitale Medien
    Digitale Medien
    Springer
    The journal of membrane biology 77 (1984), S. 277-283 
    ISSN: 1432-1424
    Schlagwort(e): hemocyanin ; channel selectivity ; energy barriers ; ion transport
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Summary The selectivity of the hemocyanin channel was measured for alkali metal ions and ammonium. Permeability ratios relative to K+ measured from biionic potentials were: NH 4 + (1.52)〉Rb+ (1.05)〉K+ (1.0)〉Cs+ (0.89)〉Na+ (0.81)〉Li+ (0.35). Single-channel ion conductance was a saturating function of ion concentration regardless of the cation present in the bathing medium. Maximal conductances were 270, 267, 215, 176, 170 and 37 ps for K+, Rb+, NH 4 + , Cs+, Na+ and Li+, respectively. Current-voltage curves for the different monovalent cations were measured and described using a threebarrier model previously used to explain the voltage dependence of the “instantaneous” channel conductance (Cecchi, Alvarez & Latorre, 1981). In this way, binding and peak energies were estimated for the different ions. Considering the energy peaks as transition states between the ion and the channel, it is concluded that they follow Eisenman's selectivity sequences XI (cis peak, i.e., Li+〉Na+〉K+〉Rb+〉Cs+; highest field strength), VII (central peak) and II (trans peak). The cis side was that to which hemocyanin was added and was electrically ground. The binding energies, on the other hand, follow Eisenman's series XI for strong electric field sites. Binding of NH 4 + to the cis-well suggests that the orientation of the ligands in the site is tetrahedric.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 7
    ISSN: 1432-1424
    Schlagwort(e): surface charge ; potassium channel ; calcium ; phosphatidylserine ; planar bilayer
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Summary A Ca-activated, K-selective channel from plasma membrane of rat skeletal muscle was studied in artificial lipid bilayers formed from either phosphatidylethanolamine (PE) or phosphatidylserine (PS). In PE, the single-channel conductance exhibited a complex dependence on symmetrical K+ concentration that could not be described by simple Michaelis-Menten saturation. At low K+ concentrations the channel conductance was higher in PS membranes, but approached the same conductance observed in PE above 0.4m KCl. At the same Ca2+ concentration and voltage, the probability of channel opening was significantly greater in PS than PE. The differences in the conduction and gating, observed in the two lipids, can be explained by the negative surface charge of PS compared to the neutral PE membrane. Model calculations of the expected concentrations of K+ and Ca2+ at various distances from a PS membrane surface, using Gouy-Chapman-Stern theory, suggest that the K+-conduction and Ca2+-activation sites sense a similar fraction of the surface potential, equivalent to the local electrostatic potential at a distance of 9 Å from the surface.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 8
    Digitale Medien
    Digitale Medien
    Springer
    Journal of inclusion phenomena and macrocyclic chemistry 12 (1992), S. 23-53 
    ISSN: 1573-1111
    Schlagwort(e): Molecular dynamics ; free energy perturbation simulations ; ion-binding ion-complexation ; ion-selectivity ; ion-carbonyl bond angles and distances ; valinomycin selectivity ; MOLARIS ; GROMOS ; Pedersen two-phase salt-extraction ; Eisenman selectivity sequences ; Lennard-Jones parameters for ions ; isostericity
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract Experimental values of the free energies of cation binding to the cyclic depsipeptide molecule, valinomycin, obtained from Pedersen-type salt extraction measurements, provide data against which it is possible to test the adequacy of the procedures and force fields of the molecular dynamics algorithms, MOLARIS and GROMOS. These data are then used to assess appropriate values for the partial charges of the ester carbonyl oxygen and carbon. Valinomycin was chosen because it has only one kind of ion-binding ligand and because the cation is sufficiently enfolded by the molecule in the ion-complexes that the overall size and shape of the complex is virtually the same regardless of the species of cation bound. For such an ‘isosteric complex’, the experimentally measured selectivities are sufficiently similar in a wide variety of solvent environments that thedifferences in free energies measured between the different ion-valinomycin complexes by two-phase salt extraction experiments into dichloromethane can be taken as equivalent to the differences in free energies in vacuo. Thesedifferences were therefore compared with those computed for ion-valinomycin complexationin vacuo by Free Energy Perturbation/Molecular Dynamics (FEP/MD) simulations using the MOLARIS and GROMOS programs. Starting with a set of Lennard-Jones 6–12 parameters for the monovalent cations assessed for aqueous solution we explored the effect of varying the partial charges of the ester carbonyl ligands on binding free energy differences (i.e. the selectivity) among Na, K, Rb, and Cs. The computed selectivity was found to depend strongly on the value of partial charge, following a typical ‘Eisenman Selectivity Pattern’ in which the correct selectivity sequence and magnitude occurred only over a very narrow range of partial charge (around 0.33 and 0.6 for the standard carbonyls of MOLARIS and GROMOS, respectively). Using MOLARIS we explored the effect of varying the size of the ester carbonyl ligands by comparing the standard carbonyl of MOLARIS with the somewhat smaller carbonyls of GROMOS and found an equally satisfactory ability to reproduce the experimental data with a partial charge value of 0.41. These results validate the use of both the MOLARIS and GROMOS force fields as starting points for quantitative calculations of ion-binding in more complex molecules (e.g., ion-binding sites and channels in proteins).
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 9
    Publikationsdatum: 2018-08-20
    Beschreibung: The voltage-gated proton (Hv1) channel, a voltage sensor and a conductive pore contained in one structural module, plays important roles in many physiological processes. Voltage sensor movements can be directly detected by measuring gating currents, and a detailed characterization of Hv1 charge displacements during channel activation can help to understand the function of this channel. We succeeded in detecting gating currents in the monomeric form of the Ciona-Hv1 channel. To decrease proton currents and better separate gating currents from ion currents, we used the low-conducting Hv1 mutant N264R. Isolated ON-gating currents decayed at increasing rates with increasing membrane depolarization, and the amount of gating charges displaced saturates at high voltages. These are two hallmarks of currents arising from the movement of charged elements within the boundaries of the cell membrane. The kinetic analysis of gating currents revealed a complex time course of the ON-gating current characterized by two peaks and a marked Cole–Moore effect. Both features argue that the voltage sensor undergoes several voltage-dependent conformational changes during activation. However, most of the charge is displaced in a single central transition. Upon voltage sensor activation, the charge is trapped, and only a fast component that carries a small percentage of the total charge is observed in the OFF. We hypothesize that trapping is due to the presence of the arginine side chain in position 264, which acts as a blocking ion. We conclude that the movement of the voltage sensor must proceed through at least five states to account for our experimental data satisfactorily.
    Print ISSN: 0027-8424
    Digitale ISSN: 1091-6490
    Thema: Biologie , Medizin , Allgemeine Naturwissenschaft
    Standort Signatur Erwartet Verfügbarkeit
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  • 10
    Publikationsdatum: 2003-11-01
    Print ISSN: 0300-8177
    Digitale ISSN: 1573-4919
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Publiziert von Springer
    Standort Signatur Erwartet Verfügbarkeit
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