Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.
about
Tryptophan-lipid interactions in membrane protein folding probed by ultraviolet resonance Raman and fluorescence spectroscopy.Effects of clinically relevant MPL mutations in the transmembrane domain revealed at the atomic level through computational modeling.Single tryptophan and tyrosine comparisons in the N-terminal and C-terminal interface regions of transmembrane GWALP peptidesComparisons of interfacial Phe, Tyr, and Trp residues as determinants of orientation and dynamics for GWALP transmembrane peptides.Helical distortion in tryptophan- and lysine-anchored membrane-spanning alpha-helices as a function of hydrophobic mismatch: a solid-state deuterium NMR investigation using the geometric analysis of labeled alanines methodIs there a preferential interaction between cholesterol and tryptophan residues in membrane proteins?The preference of tryptophan for membrane interfaces: insights from N-methylation of tryptophans in gramicidin channelsCharged or aromatic anchor residue dependence of transmembrane peptide tilt.Bayesian classification of residues associated with protein functional divergence: Arf and Arf-like GTPases.A Conserved Residue Cluster That Governs Kinetics of ATP-dependent Gating of Kir6.2 Potassium ChannelsIsotope labeling for solution and solid-state NMR spectroscopy of membrane proteinsNovel pH-Sensitive Cyclic PeptidesOrientation and dynamics of transmembrane peptides: the power of simple models.Coarse grained molecular dynamics simulations of transmembrane protein-lipid systems.Response of GWALP transmembrane peptides to changes in the tryptophan anchor positions.Canonical azimuthal rotations and flanking residues constrain the orientation of transmembrane helices.Emerging complexities of lipid regulation of potassium channels.Peptide adsorption to lipid bilayers: slow processes revealed by linear dichroism spectroscopy.The membrane interface dictates different anchor roles for "inner pair" and "outer pair" tryptophan indole rings in gramicidin A channels.Properties of membrane-incorporated WALP peptides that are anchored on only one end.Tyrosine replacing tryptophan as an anchor in GWALP peptides.Concerning tryptophan and protein-bilayer interactionsComparison of "Polarization inversion with spin exchange at magic angle" and "geometric analysis of labeled alanines" methods for transmembrane helix alignment.New applications of solid-state NMR in structural biology
P2860
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P2860
Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.
@en
Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.
@nl
type
label
Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.
@en
Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.
@nl
prefLabel
Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.
@en
Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.
@nl
P2860
P50
P356
P1433
P1476
Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides
@en
P2093
Nicole D Reed
P2860
P304
P356
10.1021/BI700082V
P407
P577
2007-05-27T00:00:00Z