title: The temperature dependence of gramicidin conformational States in octanol.
abstract: In lipid bilayers and organic solvents, the hydrophobic polypeptide gramicidin adopts a number of different conformations, some of which are capable of conducting monovalent cations across phospholipid membranes. The equilibria between conformations have been shown to be influenced by factors such as lipid chain length, solvent, concentration and salt. In this study, the temperature dependence of the equilibrium mixture of double helical ion-free gramicidin in octanol was examined using circular dichroism spectroscopy.
authors.affiliation: Department of Crystallography, Birkbeck College, University of London, London WC1E 7HX UK.
authors.forename: Farah
authors.initials: F
authors.lastname: O'Boyle
authors.forename: B A
authors.initials: BA
authors.lastname: Wallace
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry; D002942:Circular Dichroism; D003627:Data Interpretation, Statistical; D006096:Gramicidin / Q000737:chemistry*; D008969:Molecular Sequence Data; D000442:Octanols / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship; D013696:Temperature
chemical_list: D000900:Anti-Bacterial Agents; D000442:Octanols; D006096:Gramicidin