An innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies.
about
MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain.Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubesThe magic of bicelles lights up membrane protein structureStructure and Membrane Interactions of the Antibiotic Peptide Dermadistinctin K by Multidimensional Solution and Oriented 15N and 31P Solid-State NMR SpectroscopyNMR Structure of Pardaxin, a Pore-forming Antimicrobial Peptide, in Lipopolysaccharide Micelles: MECHANISM OF OUTER MEMBRANE PERMEABILIZATIONA refinement protocol to determine structure, topology, and depth of insertion of membrane proteins using hybrid solution and solid-state NMR restraints.Membrane interactions of phylloseptin-1, -2, and -3 peptides by oriented solid-state NMR spectroscopy.Deletion of all cysteines in tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and lipopolysaccharide selective bindingFreezing point depression of water in phospholipid membranes: a solid-state NMR study.Antimicrobial and membrane disrupting activities of a peptide derived from the human cathelicidin antimicrobial peptide LL37Orientation, dynamics, and lipid interaction of an antimicrobial arylamide investigated by 19F and 31P solid-state NMR spectroscopy.Membrane-bound dynamic structure of an arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR.Oriented samples: a tool for determining the membrane topology and the mechanism of action of cationic antimicrobial peptides by solid-state NMR.Limiting an antimicrobial peptide to the lipid-water interface enhances its bacterial membrane selectivity: a case study of MSI-367Chemical shift tensor - the heart of NMR: Insights into biological aspects of proteinsMembrane composition determines pardaxin's mechanism of lipid bilayer disruption.Role of cationic group structure in membrane binding and disruption by amphiphilic copolymersOrientation of a beta-hairpin antimicrobial peptide in lipid bilayers from two-dimensional dipolar chemical-shift correlation NMR.Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin.Structure and orientation of pardaxin determined by NMR experiments in model membranes.Flow-through lipid nanotube arrays for structure-function studies of membrane proteins by solid-state NMR spectroscopy.Membrane interaction of antimicrobial peptides using E. coli lipid extract as model bacterial cell membranes and SFG spectroscopyStructure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studiesHigh-resolution 2D NMR spectroscopy of bicelles to measure the membrane interaction of ligands.Preparation of oriented, fully hydrated lipid samples for structure determination using X-ray scattering.When detergent meets bilayer: birth and coming of age of lipid bicelles.Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights.Effect of membrane composition on antimicrobial peptides aurein 2.2 and 2.3 from Australian southern bell frogsStructure, membrane orientation, mechanism, and function of pexiganan--a highly potent antimicrobial peptide designed from magainin.High-resolution NMR field-cycling device for full-range relaxation and structural studies of biopolymers on a shared commercial instrument.Cholesterol reduces pardaxin's dynamics-a barrel-stave mechanism of membrane disruption investigated by solid-state NMR.Antimicrobial activity and membrane selective interactions of a synthetic lipopeptide MSI-843Optimizing oriented planar-supported lipid samples for solid-state protein NMR.Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.Asymmetric insertion of membrane proteins in lipid bilayers by solid-state NMR paramagnetic relaxation enhancement: a cell-penetrating Peptide exampleStructural determinants of antimicrobial and antiplasmodial activity and selectivity in histidine-rich amphipathic cationic peptides.Resolution enhancement in solid-state NMR of oriented membrane proteins by anisotropic differential linebroadening.A spectroscopic study of the membrane interaction of the antimicrobial peptide Pleurocidin.Impact of membrane curvature on amyloid aggregation.
P2860
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P2860
An innovative procedure using a sublimable solid to align lipid bilayers for solid-state NMR studies.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
An innovative procedure using ...... s for solid-state NMR studies.
@ast
An innovative procedure using ...... s for solid-state NMR studies.
@en
An innovative procedure using ...... s for solid-state NMR studies.
@nl
type
label
An innovative procedure using ...... s for solid-state NMR studies.
@ast
An innovative procedure using ...... s for solid-state NMR studies.
@en
An innovative procedure using ...... s for solid-state NMR studies.
@nl
prefLabel
An innovative procedure using ...... s for solid-state NMR studies.
@ast
An innovative procedure using ...... s for solid-state NMR studies.
@en
An innovative procedure using ...... s for solid-state NMR studies.
@nl
P2093
P2860
P1433
P1476
An innovative procedure using ...... s for solid-state NMR studies.
@en
P2093
Ayyalusamy Ramamoorthy
Dong-Kuk Lee
Katherine Henzler Wildman
Kevin J Hallock
P2860
P304
P356
10.1016/S0006-3495(02)75592-6
P407
P577
2002-05-01T00:00:00Z