title: Influence of the nature of the aromatic side-chain on the conductance of the channel of linear gramicidin: study of a series of 9,11,13,15-Tyr(O-protected) derivatives.
abstract: This paper describes the single channel properties of a series of synthetic analogues of gramicidin A, where all four tryptophans are replaced either by tyrosine or by several O-protected (benzyl, methyl, ethyl or t-butyl) derivatives. It is shown that, although all analogues bear similar dipole moment on their side-chains, the conductance depends on the hydrophobicity of these protecting groups. An analysis of the conductance data suggests that the conductance is governed by the binding process and a possible explanation, based on conformational considerations, is proposed.
authors.affiliation: CRBM, CNRS/INSERM, Montpellier, France.
authors.forename: D
authors.initials: D
authors.lastname: Benamar
authors.forename: P
authors.initials: P
authors.lastname: Daumas
authors.forename: Y
authors.initials: Y
authors.lastname: Trudelle
authors.forename: B
authors.initials: B
authors.lastname: Calas
authors.forename: R
authors.initials: R
authors.lastname: Bennes
authors.forename: F
authors.initials: F
authors.lastname: Heitz
mesh_terms: D000595:Amino Acid Sequence; D004553:Electric Conductivity; D006096:Gramicidin / Q000737:chemistry*; D007473:Ion Channels / Q000737:chemistry / Q000502:physiology; D008563:Membrane Lipids / Q000737:chemistry / Q000502:physiology; D008566:Membranes / Q000737:chemistry / Q000502:physiology; D008969:Molecular Sequence Data; D013329:Structure-Activity Relationship; D014364:Tryptophan / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry*
chemical_list: D007473:Ion Channels; D008563:Membrane Lipids; D006096:Gramicidin; D014443:Tyrosine; D014364:Tryptophan