Membrane structure of voltage-gated channel forming peptides by site-directed spin-labeling.
about
The role of hydrophobic interactions in positioning of peripheral proteins in membranesTOAC spin labels in the backbone of alamethicin: EPR studies in lipid membranesSpatial structure of zervamicin IIB bound to DPC micelles: implications for voltage-gatingWhat Ion Flow along Ion Channels Can Tell us about Their Functional ActivityConformation of alamethicin in oriented phospholipid bilayers determined by (15)N solid-state nuclear magnetic resonance.Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces.Genetically engineered metal ion binding sites on the outside of a Channel's transmembrane beta-barrel.The role of proline and glycine in determining the backbone flexibility of a channel-forming peptide.Continuum solvent model calculations of alamethicin-membrane interactions: thermodynamic aspects.Structural features that modulate the transmembrane migration of a hydrophobic peptide in lipid vesiclesAntimicrobial peptides in toroidal and cylindrical pores.Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domainsOrientation of the pore-forming peptide GALA in POPC vesicles determined by a BODIPY-avidin/biotin binding assay.Melittin-induced bilayer leakage depends on lipid material properties: evidence for toroidal pores.Structure and alignment of the membrane-associated peptaibols ampullosporin A and alamethicin by oriented 15N and 31P solid-state NMR spectroscopy.Hydrogen bonding in helical polypeptides from molecular dynamics simulations and amide hydrogen exchange analysis: alamethicin and melittin in methanol.Calculations suggest a pathway for the transverse diffusion of a hydrophobic peptide across a lipid bilayer.Alamethicin helices in a bilayer and in solution: molecular dynamics simulations.Peptaibol zervamicin IIb structure and dynamics refinement from transhydrogen bond J couplings.Simulation studies of alamethicin-bilayer interactions.Intrinsic rectification of ion flux in alamethicin channels: studies with an alamethicin dimer.A thermodynamic approach to alamethicin pore formationInfluence of proline position upon the ion channel activity of alamethicin.Lipid chain-length dependence for incorporation of alamethicin in membranes: electron paramagnetic resonance studies on TOAC-spin labeled analogs.
P2860
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P2860
Membrane structure of voltage-gated channel forming peptides by site-directed spin-labeling.
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Membrane structure of voltage- ...... y site-directed spin-labeling.
@ast
Membrane structure of voltage- ...... y site-directed spin-labeling.
@en
type
label
Membrane structure of voltage- ...... y site-directed spin-labeling.
@ast
Membrane structure of voltage- ...... y site-directed spin-labeling.
@en
prefLabel
Membrane structure of voltage- ...... y site-directed spin-labeling.
@ast
Membrane structure of voltage- ...... y site-directed spin-labeling.
@en
P356
P1433
P1476
Membrane structure of voltage- ...... y site-directed spin-labeling.
@en
P2093
Barranger-Mathys M
P304
P356
10.1021/BI951985D
P407
P577
1996-01-01T00:00:00Z