Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
about
Importance of indole N-H hydrogen bonding in the organization and dynamics of gramicidin channels.Conformational trapping in a membrane environment: a regulatory mechanism for protein activity?Conformation of gramicidin A in Triton X-100 micelles from CD and FTIR data: a clean example of antiparallel double β5.6 helix formation.Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.The preference of tryptophan for membrane interfaces: insights from N-methylation of tryptophans in gramicidin channelsProtein stability and conformational rearrangements in lipid bilayers: linear gramicidin, a model system.On the supramolecular organization of gramicidin channels. The elementary conducting unit is a dimerOptimizing and characterizing alignment of oriented lipid bilayers containing gramicidin DGramicidin single-channel properties show no solvent-history dependence.Gramicidins A, B, and C form structurally equivalent ion channels.Spectroscopic [correction of eSpectroscopic] and structural properties of valine gramicidin A in monolayers at the air-water interface.Spin-labeled gramicidin a: channel formation and dissociation.Channel and nonchannel forms of spin-labeled gramicidin in membranes and their equilibria.Role of tryptophan residues in gramicidin channel organization and function.The gramicidin dimer shows both EX1 and EX2 mechanisms of H/D exchange.The structure of an integral membrane peptide: a deuterium NMR study of gramicidin.Dynamics of an integral membrane peptide: a deuterium NMR relaxation study of gramicidin.Distinguishing gramicidin D conformers through two-dimensional infrared spectroscopy of vibrational excitons.13C solid-state NMR of gramicidin A in a lipid membrane.Monitoring gramicidin conformations in membranes: a fluorescence approach.Effect of graded hydration on the dynamics of an ion channel peptide: a fluorescence approach.Solvent history dependence of gramicidin-lipid interactions: a Raman and infrared spectroscopic study.Hydration at the membrane protein-lipid interface.Effect of structural transition of the host assembly on dynamics of an ion channel peptide: a fluorescence approach.New fluorescent octadecapentaenoic acids as probes of lipid membranes and protein-lipid interactions.High-speed magic angle spinning solid-state 1H nuclear magnetic resonance study of the conformation of gramicidin A in lipid bilayers.A semi-empirical approach for the simulation of circular dichroism spectra of gramicidin A in a model membrane.
P2860
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P2860
Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
description
1988 nî lūn-bûn
@nan
1988 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
@ast
Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
@en
Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
@nl
type
label
Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
@ast
Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
@en
Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
@nl
prefLabel
Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
@ast
Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
@en
Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
@nl
P2093
P2860
P1433
P1476
Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(88)82955-2
P407
P577
1988-08-01T00:00:00Z