Solid-state 15N NMR of oriented lipid bilayer bound gramicidin A'.
about
Structure determination of membrane proteins by nuclear magnetic resonance spectroscopyStructure Determination of a Membrane Protein in ProteoliposomesThe conducting form of gramicidin A is a right-handed double-stranded double helixThe development of solid-state NMR of membrane proteins.Steric interactions of valines 1, 5, and 7 in [valine 5, D-alanine 8] gramicidin A channels.Orientation and dynamics of an antimicrobial peptide in the lipid bilayer by solid-state NMR spectroscopy.Raman linear intensity difference of membrane-bound peptides: indole ring orientations of tryptophans 11 and 13 in the gramicidin A transmembrane channel.Solid-phase peptide synthesis and solid-state NMR spectroscopy of [Ala3-15N][Val1]gramicidin A.Gramicidin D conformation, dynamics and membrane ion transport.Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteins2H NMR determination of the global correlation time of the gramicidin channel in a lipid bilayerSpecies heterogeneity of Gly-11 gramicidin A incorporated into sodium dodecyl sulfate micelles.Side-chain structure and dynamics at the lipid-protein interface: Val1 of the gramicidin A channel.Optimizing and characterizing alignment of oriented lipid bilayers containing gramicidin DAn innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies.Structural restraints and heterogeneous orientation of the gramicidin A channel closed state in lipid bilayers.Dynamic structure of vesicle-bound melittin in a variety of lipid chain lengths by solid-state NMR.Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers.Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy.Solid-state NMR and membrane proteins.Validation of the single-stranded channel conformation of gramicidin A by solid-state NMR.Mechanically, magnetically, and "rotationally aligned" membrane proteins in phospholipid bilayers give equivalent angular constraints for NMR structure determination.Orientations of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy.Determination of the structure of a membrane-incorporated ion channel. Solid-state nuclear magnetic resonance studies of gramicidin AOrientational constraints as three-dimensional structural constraints from chemical shift anisotropy: the polypeptide backbone of gramicidin A in a lipid bilayer.Sodium ion binding in the gramicidin A channel. Solid-state NMR studies of the tryptophan residues
P2860
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P2860
Solid-state 15N NMR of oriented lipid bilayer bound gramicidin A'.
description
1987 nî lūn-bûn
@nan
1987 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Solid-state 15N NMR of oriented lipid bilayer bound gramicidin A'.
@ast
Solid-state 15N NMR of oriented lipid bilayer bound gramicidin A'.
@en
type
label
Solid-state 15N NMR of oriented lipid bilayer bound gramicidin A'.
@ast
Solid-state 15N NMR of oriented lipid bilayer bound gramicidin A'.
@en
prefLabel
Solid-state 15N NMR of oriented lipid bilayer bound gramicidin A'.
@ast
Solid-state 15N NMR of oriented lipid bilayer bound gramicidin A'.
@en
P2093
P356
P1433
P1476
Solid-state 15N NMR of oriented lipid bilayer bound gramicidin A'.
@en
P2093
P304
P356
10.1021/BI00395A009
P407
P577
1987-10-01T00:00:00Z