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Temperature dependence of single channel currents and the peptide libration mechanism for ion transport through the gramicidin A transmembrane channel

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Summary

A study of the temperature dependence of gramicidin A conductance of K+ in diphytanoyllecithin/n-decane membranes shows the plot of In (single channel conductance) as a function of reciprocal temperature to be nonlinear for the most probable set of conductance, states. These results are considered in terms of a series of barriers, of the dynamics of channel conformation,vis-a-vis the peptide libration mechanism, and of the effect of lipid viscosity on side chain motions again as affecting the energetics of peptide libration.

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Authors and Affiliations

  1. Laboratory of Molecular Biophysics, University of Alabama in Birmingham, School of Medicine, 35294, Birmingham, Alabama

    D. W. Urry, S. Alonso-Romanowski, C. M. Venkatachalam & R. D. Harris

  2. Neurosciences Program, University of Alabama in Birmingham, School of Medicine, 35294, Birmingham, Alabama

    R. J. Bradley

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  1. D. W. Urry
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  2. S. Alonso-Romanowski
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  3. C. M. Venkatachalam
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  4. R. J. Bradley
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  5. R. D. Harris
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Urry, D.W., Alonso-Romanowski, S., Venkatachalam, C.M. et al. Temperature dependence of single channel currents and the peptide libration mechanism for ion transport through the gramicidin A transmembrane channel. J. Membrain Biol. 81, 205–217 (1984). https://doi.org/10.1007/BF01868714

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  • DOI: https://doi.org/10.1007/BF01868714

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