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Theoretical analysis of gramicidin A transmembrane channel. II. Energetics of helical librational states of the channel

โœ Scribed by C. M. Venkatachalam; D. W. Urry

Publisher
John Wiley and Sons
Year
1984
Tongue
English
Weight
687 KB
Volume
5
Category
Article
ISSN
0192-8651

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โœฆ Synopsis

The degrees of conformational freedom of poly GD P-helicd chain are analyzed consistent with the helical parameters of gramicidin A structure. From conformational energy calculations, " helical librations" that can be sustained by this structure are described and the energy of libration a s a function of the cavity size is presented. Two different modes of conformational change are identified corresponding to librations of all L-D-peptide units or all D-L-peptide units while retaining the helical parameters. Such helical librations are considered relative to conformational perturbations due to the presence of an ion in the channel,

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