NMR methods for studying membrane-active antimicrobial peptides
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Functional and Structural Insights of a Staphylococcus aureus Apoptotic-like Membrane Peptide from a Toxin-Antitoxin ModuleToward an improved structural model of the frog-skin antimicrobial peptide esculentin-1b(1-18).The singular behavior of a β-type semi-synthetic two branched polypeptide: three-dimensional structure and mode of action.Oriented samples: a tool for determining the membrane topology and the mechanism of action of cationic antimicrobial peptides by solid-state NMR.Characterization of sodium dodecylsulphate and dodecylphosphocholine mixed micelles through NMR and dynamic light scattering.Enhanced amphiphilic profile of a short β-stranded peptide improves its antimicrobial activity.Initial Molecular Recognition Steps of McjA Precursor during Microcin J25 Lasso Peptide Maturation.Arginine-, D-arginine-vasopressin, and their inverso analogues in micellar and liposomic models of cell membrane: CD, NMR, and molecular dynamics studies.Membrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design.Position-Dependent Influence of the Three Trp Residues on the Membrane Activity of the Antimicrobial Peptide, Tritrpticin.Ocellatin peptides from the skin secretion of the South American frog Leptodactylus labyrinthicus (Leptodactylidae): characterization, antimicrobial activities and membrane interactions.Molecular mechanism of synergy between the antimicrobial peptides PGLa and magainin 2.Peptide model helices in lipid membranes: insertion, positioning, and lipid response on aggregation studied by X-ray scattering.Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.A kinked antimicrobial peptide from Bombina maxima. II. Behavior in phospholipid bilayers.Influence of hydrophobic residues on the activity of the antimicrobial peptide magainin 2 and its synergy with PGLa.Sterols associated with small unilamellar vesicles (SUVs): intrinsic mobility role for 1H NMR detectionStructural Framework for the Modulation of the Activity of the Hybrid Antibiotic Peptide Cecropin A-Melittin [CA(1-7)M(2-9)] by Nε-Lysine TrimethylationHomo- and heteromeric interaction strengths of the synergistic antimicrobial peptides PGLa and magainin 2 in membranes
P2860
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P2860
NMR methods for studying membrane-active antimicrobial peptides
description
wetenschappelijk artikel
@nl
наукова стаття, опублікована в листопаді 2004
@uk
name
NMR methods for studying membrane-active antimicrobial peptides
@en
NMR methods for studying membrane-active antimicrobial peptides
@nl
type
label
NMR methods for studying membrane-active antimicrobial peptides
@en
NMR methods for studying membrane-active antimicrobial peptides
@nl
prefLabel
NMR methods for studying membrane-active antimicrobial peptides
@en
NMR methods for studying membrane-active antimicrobial peptides
@nl
P356
P1476
NMR methods for studying membrane-active antimicrobial peptides
@en
P304
P356
10.1002/CMR.A.20024
P577
2004-11-09T00:00:00Z