The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy

Biochimica et Biophysica Acta - Biomembranes

Volumn 1462, Issue 1-2, 1999, Pages 157-183

  Bechinger, Burkhard ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Alamethicin; Amphipathic peptide; Cecropin; Dermaseptin; Gramic idin A; Magainin; Melittin; Peptide pore formation; Phospholipid membrane; Polypeptide lipid interaction; Regulation; Selectivity

Indexed keywords

ALAMETHICIN; CECROPIN; DERMASEPTIN; GRAMICIDIN A; MAGAININ DERIVATIVE; MELITTIN; PEPTIDE DERIVATIVE;

ANTIMICROBIAL ACTIVITY; CHANNEL GATING; DRUG CONFORMATION; DRUG SYNTHESIS; LIPID MEMBRANE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE; REGULATORY MECHANISM; REVIEW; STRUCTURE ACTIVITY RELATION;

ALAMETHICIN; AMINO ACID SEQUENCE; AMPHIBIA; ANIMALS; ANTI-INFECTIVE AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; DRUG DESIGN; GRAMICIDIN; INSECTS; LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; MELITTEN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS PROTEINS;

AMPHIBIA; HEXAPODA;

EID: 0032717887     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(99)00205-9     Document Type: Review

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