Gramicidin channels--a solvable membrane "protein" folding problem.
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.
Andersen
O S
OS
Department of Physiology and Biophysics, Cornell University Medical College, New York, NY 10021, USA.
Saberwal
G
G
Greathouse
D V
DV
Koeppe
R E
RE
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
D007473:Ion Channels; D008051:Lipid Bilayers; D008565:Membrane Proteins; D006096:Gramicidin