Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an α-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution

Journal of Biomolecular NMR

Volumn 9, Issue 2, 1997, Pages 127-135

  Gesell, Jennifer ^a   Zasloff, Michael ^b   Opella, Stanley J ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b Genaera Corporation   (United States)

Author keywords

Amphipathic helix; Magainin; Membrane; Micelle

Indexed keywords

ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; DEUTERIUM; DODECYL SULFATE SODIUM; DODECYLPHOSPHORYLCHOLINE; DRUG DERIVATIVE; HYDROGEN; MAGAININ 2 PEPTIDE, XENOPUS; PEPTIDE; PHOSPHORYLCHOLINE; TRIFLUOROETHANOL; WATER; XENOPUS PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; METHODOLOGY; MICELLE; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN SECONDARY STRUCTURE; SOLUTION AND SOLUBILITY; SYNTHESIS;

AMINO ACID SEQUENCE; ANTI-INFECTIVE AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; DEUTERIUM; HYDROGEN; MAGNETIC RESONANCE SPECTROSCOPY; MICELLES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PHOSPHORYLCHOLINE; PROTEIN STRUCTURE, SECONDARY; SODIUM DODECYL SULFATE; SOLUTIONS; TRIFLUOROETHANOL; WATER; XENOPUS PROTEINS;

EID: 0031062621     PISSN: 09252738     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1018698002314     Document Type: Article

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