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Volumn 42, Issue 2, 2004, Pages 155-161

Peptide-related alterations of membrane-associated water: Deuterium solid-state NMR investigations of phosphatidylcholine membranes at different hydration levels

(2) Moraes, Cléria Mendonça a,b Bechinger, Burkhard a,b

a UNIVERSITÉ DE STRASBOURG (France)

b MAX PLANCK INSTITUTE OF BIOCHEMISTRY (Germany)

Author keywords

2H NMR; Amphipathic peptide; Antimicrobial peptides; Channel; Fusion; LAH4; M2; NMR; Phospholipid bilayer surface; Pore; S4; Transmembrane sequence; Water lipid interface

Indexed keywords

AMINO ACIDS; DEUTERIUM; HYDRATION; LIGHT POLARIZATION; LIPID BILAYERS; MICROORGANISMS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHASE INTERFACES; PHOSPHOLIPIDS;

2H NMR; AMPHIPATHIC PEPTIDES; ANTIMICROBIAL PEPTIDE; BILAYER SURFACE; CHANNEL; LAH4; M2; PHOSPHOLIPID BILAYER SURFACE; PHOSPHOLIPIDS BILAYER; PORE; TRANSMEMBRANE SEQUENCES; WATER-LIPID INTERFACE;

PEPTIDES;

DEUTERIUM; MEMBRANE PROTEIN; PEPTIDE; PHOSPHATIDYLCHOLINE; PHOSPHORUS 31; PROTON; WATER;

AMINO ACID SEQUENCE; BILAYER MEMBRANE; CONFERENCE PAPER; DEUTERON NUCLEAR MAGNETIC RESONANCE; HUMIDITY; HYDRATION; INFLUENZA A; LIPID COMPOSITION; LIPID MEMBRANE; MEMBRANE PERMEABILITY; MOLECULAR MODEL; PHOSPHORUS NUCLEAR MAGNETIC RESONANCE; PROTEIN DOMAIN; QUANTITATIVE ANALYSIS; SAMPLING; SODIUM CHANNEL;

EID: 0842329185 PISSN: 07491581 EISSN: None Source Type: Journal
DOI: 10.1002/mrc.1321 Document Type: Conference Paper

Times cited : (17)

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