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Volumn 269, Issue 16, 2002, Pages 3869-3880
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Structures and mode of membrane interaction of a short α helical lytic peptide and its diastereomer determined by NMR, FTIR, and fluorescence spectroscopy
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Author keywords
Cytolytic peptides; Membrane permeation; Peptide membrane interactions; Polydiacetylene
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Indexed keywords
AMINO ACID;
AMPHOLYTE;
DODECYL SULFATE SODIUM;
DODECYLPHOSPHORYLCHOLINE;
PEPTIDE;
PHOSPHOLIPID;
TRYPTOPHAN;
ALPHA HELIX;
ARTICLE;
BETA SHEET;
BROMINATION;
CALCULATION;
CHEMICAL INTERACTION;
COLORIMETRY;
DIASTEREOISOMER;
FLUORESCENCE SPECTROSCOPY;
HYDROPHOBICITY;
INFRARED SPECTROSCOPY;
LIPID BILAYER;
MEMBRANE BINDING;
MEMBRANE TRANSPORT;
MICELLE;
NUCLEAR MAGNETIC RESONANCE;
PEPTIDE ANALYSIS;
PRIORITY JOURNAL;
PROTEIN STRUCTURE;
SEGREGATION ANALYSIS;
AMINO ACID SEQUENCE;
COLORIMETRY;
HYDROPHOBICITY;
LIPID BILAYERS;
MICELLES;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;
PEPTIDES;
PHOSPHORYLCHOLINE;
PROTEIN STRUCTURE, SECONDARY;
SODIUM DODECYL SULFATE;
SPECTROMETRY, FLUORESCENCE;
SPECTROSCOPY, FOURIER TRANSFORM INFRARED;
STEREOISOMERISM;
STRUCTURE-ACTIVITY RELATIONSHIP;
TRYPTOPHAN;
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EID: 0036038922
PISSN: 00142956
EISSN: None
Source Type: Journal
DOI: 10.1046/j.1432-1033.2002.03080.x Document Type: Article |
Times cited : (82)
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References (54)
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