title: The conformational preference of gramicidin channels is a function of lipid bilayer thickness.
abstract: 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.
authors.affiliation: Department of Physiology and Biophysics, Cornell University Medical College, New York, NY 10021, USA.
authors.forename: N
authors.initials: N
authors.lastname: Mobashery
authors.forename: C
authors.initials: C
authors.lastname: Nielsen
authors.forename: O S
authors.initials: OS
authors.lastname: Andersen
mesh_terms: 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
chemical_list: D007473:Ion Channels; D008051:Lipid Bilayers; D006096:Gramicidin; D000431:Ethanol; D004121:Dimethyl Sulfoxide