Influence of flanking residues on tilt and rotation angles of transmembrane peptides in lipid bilayers. A solid-state 2H NMR study.
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Revisiting hydrophobic mismatch with free energy simulation studies of transmembrane helix tilt and rotationDetermining the orientation and localization of membrane-bound peptidesInfluence of trifluoroethanol on membrane interfacial anchoring interactions of transmembrane alpha-helical peptides.Interpretation of 2H-NMR experiments on the orientation of the transmembrane helix WALP23 by computer simulations.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 methodEffect of sequence hydrophobicity and bilayer width upon the minimum length required for the formation of transmembrane helices in membranes.Orientation and dynamics of peptides in membranes calculated from 2H-NMR dataOrder parameters of a transmembrane helix in a fluid bilayer: case study of a WALP peptideChanges in transmembrane helix alignment by arginine residues revealed by solid-state NMR experiments and coarse-grained MD simulations.Transmembrane helix dynamics of bacterial chemoreceptors supports a piston model of signalling.Coupling of transmembrane helix orientation to membrane release of the juxtamembrane region in FGFR3Influence of hydrophobic mismatch and amino acid composition on the lateral diffusion of transmembrane peptides.Charged or aromatic anchor residue dependence of transmembrane peptide tilt.Mechanism of activation of protein kinase JAK2 by the growth hormone receptor.Solid-state NMR ensemble dynamics as a mediator between experiment and simulationCharacterization of the resting MscS: modeling and analysis of the closed bacterial mechanosensitive channel of small conductance.Increased hydrophobicity at the N terminus/membrane interface impairs gating of the severe combined immunodeficiency-related ORAI1 mutantTilt and rotation angles of a transmembrane model peptide as studied by fluorescence spectroscopy.Orientation and dynamics of transmembrane peptides: the power of simple models.Response of GWALP transmembrane peptides to changes in the tryptophan anchor positions.Canonical azimuthal rotations and flanking residues constrain the orientation of transmembrane helices.The Autographa californica multicapsid nucleopolyhedrovirus GP64 protein: analysis of transmembrane domain length and sequence requirements3D hydrophobic moment vectors as a tool to characterize the surface polarity of amphiphilic peptides.The Transmembrane Helix Tilt May Be Determined by the Balance between Precession Entropy and Lipid Perturbation.The dynamic orientation of membrane-bound peptides: bridging simulations and experiments.Exploring peptide-membrane interactions with coarse-grained MD simulations.Application of solid-state NMR restraint potentials in membrane protein modeling.2,2,2-Trifluoroethanol changes the transition kinetics and subunit interactions in the small bacterial mechanosensitive channel MscSMembrane bending is critical for the stability of voltage sensor segments in the membrane.Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.Lipid chain-length dependence for incorporation of alamethicin in membranes: electron paramagnetic resonance studies on TOAC-spin labeled analogs.Solid-state NMR analysis of the PGLa peptide orientation in DMPC bilayers: structural fidelity of 2H-labels versus high sensitivity of 19F-NMR.Comparison of "Polarization inversion with spin exchange at magic angle" and "geometric analysis of labeled alanines" methods for transmembrane helix alignment.Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: a systematic investigation of hydrophobic mismatch.Comparative analysis of the orientation of transmembrane peptides using solid-state (2)H- and (15)N-NMR: mobility matters.Mode of Membrane Interaction and Fusogenic Properties of ade NovoTransmembrane Model Peptide Depend on the Length of the Hydrophobic CoreA novel pH-dependent membrane peptide that binds to EphA2 and inhibits cell migration
P2860
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P2860
Influence of flanking residues on tilt and rotation angles of transmembrane peptides in lipid bilayers. A solid-state 2H NMR study.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
Influence of flanking residues ...... s. A solid-state 2H NMR study.
@en
Influence of flanking residues ...... s. A solid-state 2H NMR study.
@nl
type
label
Influence of flanking residues ...... s. A solid-state 2H NMR study.
@en
Influence of flanking residues ...... s. A solid-state 2H NMR study.
@nl
prefLabel
Influence of flanking residues ...... s. A solid-state 2H NMR study.
@en
Influence of flanking residues ...... s. A solid-state 2H NMR study.
@nl
P356
P1433
P1476
Influence of flanking residues ...... rs. A solid-state 2H NMR study
@en
P2093
J Antoinette Killian
Suat Ozdirekcan
P304
P356
10.1021/BI0481242
P407
P577
2005-01-01T00:00:00Z