Comparative analysis of the orientation of transmembrane peptides using solid-state (2)H- and (15)N-NMR: mobility matters.
about
Single tryptophan and tyrosine comparisons in the N-terminal and C-terminal interface regions of transmembrane GWALP peptidesMembrane Thinning and Thickening Induced by Membrane-Active Amphipathic Peptides.Canonical azimuthal rotations and flanking residues constrain the orientation of transmembrane helices.3D 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.Influence of glutamic acid residues and pH on the properties of transmembrane helices.Homo- and heteromeric interaction strengths of the synergistic antimicrobial peptides PGLa and magainin 2 in membranes
P2860
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P2860
Comparative analysis of the orientation of transmembrane peptides using solid-state (2)H- and (15)N-NMR: mobility matters.
description
2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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2012年学术文章
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name
Comparative analysis of the or ...... (15)N-NMR: mobility matters.
@en
Comparative analysis of the orientation of transmembrane peptides using solid-state
@nl
type
label
Comparative analysis of the or ...... (15)N-NMR: mobility matters.
@en
Comparative analysis of the orientation of transmembrane peptides using solid-state
@nl
prefLabel
Comparative analysis of the or ...... (15)N-NMR: mobility matters.
@en
Comparative analysis of the orientation of transmembrane peptides using solid-state
@nl
P2860
P50
P1476
Comparative analysis of the or ...... (15)N-NMR: mobility matters.
@en
P2093
Santiago Esteban-Martín
Stephan L Grage
P2860
P2888
P304
P356
10.1007/S00249-012-0801-0
P577
2012-03-28T00:00:00Z