title: Gramicidin channels--a solvable membrane "protein" folding problem.
abstract: The linear gramicidins are peptide antibiotics that form cation-selective channels in lipid bilayers. Gramicidin channels have very well-defined functional characteristics, and the structure of membrane-spanning gramicidin A channels is known at atomic resolution. These features make the gramicidins well suited to study how the amino acid sequence encodes the structure and function of a membrane-spanning channel. We show how one can use electrophysiological measurements to obtain structural information about conducting channels and to quantify the conformational preferences of sequence-substituted gramicidin mutants.
authors.affiliation: Department of Physiology and Biophysics, Cornell University Medical College, New York, NY 10021, USA.
authors.forename: O S
authors.initials: OS
authors.lastname: Andersen
authors.forename: G
authors.initials: G
authors.lastname: Saberwal
authors.forename: D V
authors.initials: DV
authors.lastname: Greathouse
authors.forename: R E
authors.initials: RE
authors.lastname: Koeppe
mesh_terms: D000595:Amino Acid Sequence; D006096:Gramicidin / Q000737:chemistry* / Q000494:pharmacology*; D007473:Ion Channels / Q000737:chemistry* / Q000187:drug effects*; D008051:Lipid Bilayers / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D007473:Ion Channels; D008051:Lipid Bilayers; D008565:Membrane Proteins; D006096:Gramicidin