The conformational preference of gramicidin channels is a function of lipid bilayer thickness.
In order to understand how the material properties of lipid bilayers could affect integral membrane protein function, we examined the effect of a hydrophobic mismatch on the structure and function of membrane-spanning gramicidin channels. Changes in lipid bilayer thickness affect the conformational preference of membrane-spanning gramicidin A (gA) channels (single-stranded [SS] dimers <--> double-stranded [DS] dimers) and induces an additional conductance state in the standard (SS) beta6.3-helical channel. These results provide experimental evidence for the importance of energetic coupling between the bilayer and imbedded inclusions.
Mobashery
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Department of Physiology and Biophysics, Cornell University Medical College, New York, NY 10021, USA.
Nielsen
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Andersen
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D000595:Amino Acid Sequence; D019281:Dimerization; D004121:Dimethyl Sulfoxide; D004553:Electric Conductivity; D000431:Ethanol; D006096:Gramicidin / Q000737:chemistry* / Q000378:metabolism; D007473:Ion Channels / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation
D007473:Ion Channels; D008051:Lipid Bilayers; D006096:Gramicidin; D000431:Ethanol; D004121:Dimethyl Sulfoxide