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  • Articles: DFG German National Licenses  (3)
  • Alamethicin pore  (2)
  • Calcium dependent channel  (1)
  • Channel activation  (1)
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  • Articles: DFG German National Licenses  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    The lowest conductance state of the alamethicin pore
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 596 (1980), S. 456-462 
    Details
    ISSN: 0005-2736
    Keywords: (Bilayer) ; Alamethicin pore ; Conductance state ; Ion selectivity
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2736(80)90134-0
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The gating of single calcium-dependent potassium channels is described by an activation/blockade mechanism (1982)
    Springer
    European biophysics journal 9 (1982), S. 35-60 
    Details
    ISSN: 1432-1017
    Keywords: Single channel currents ; Channel activation ; Channel blockade ; Potassium channel ; Calcium dependent channel
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Single calcium dependent potassium channels from cultured rat myoballs have been studied with the patch clamp technique, and current records subjected to statistical analysis. From the dependence of the mean open state probability on the internal calcium concentration, two calcium ions are required to open the channel. The open state and closed state lifetime distributions reveal that the usual activation model is not applicable to these channels. They are consistent with a two step gating mechanism that involves both activation by calcium and blockade by a calcium-sensitive gate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00536014
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Alamethicin pore formation: Voltage-dependent flip-flop of α-helix dipoles (1983)
    Springer
    European biophysics journal 9 (1983), S. 181-191 
    Details
    ISSN: 1432-1017
    Keywords: Alamethicin pore ; Voltage-dependent conductance ; α-helical structure ; Dipole moment ; Lipid bilayers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The voltage-dependency of alamethicin pore formation is explained by a flip-flop gating mechanism of single alamethicin molecules. The energetically preferred aggregate structure is changed from antiparallel to parallel molecule orientation by membrane voltage application. The electrical field is sensed by the permanent dipole of the α-helical molecule part which spans the hydrophobic membrane core. Ion conducting pore and pore states result from electrostatic repulsion of a varying number of parallel dipoles which arrange circularly. This model is consistent with published data and with two additional experimental facts, that pore state distributions are ionic strength dependent and pore state conductances depend on ionic current direction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00537815
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    Paper (German National Licenses)
    Fulltext
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