Toward an improved structural model of the frog-skin antimicrobial peptide esculentin-1b(1-18)

Biopolymers

Volumn 97, Issue 11, 2012, Pages 873-881

  Manzo, Giorgia ^a   Sanna, Roberta ^a   Casu, Mariano ^a   Mignogna, Giuseppina ^b   Mangoni, Maria L ^b   Rinaldi, Andrea C ^a   Scorciapino, Mariano A ^a  

^a UNIVERSITY OF CAGLIARI   (Italy)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

circular dichroism; folding propensity; frog skin peptide; NMR; TFE

Indexed keywords

3D STRUCTURE; AMPHIPATHIC; AMPHIPATHIC STRUCTURE; ANTI-MICROBIAL ACTIVITY; ANTIMICROBIAL PEPTIDE; EUKARYOTIC CELLS; EXPERIMENTAL STUDIES; FOLDING PROPENSITY; HELICAL CONFORMATION; HELICAL FOLDING; HYDROPHOBIC CLUSTERS; IN-DEPTH INVESTIGATION; INNATE IMMUNE SYSTEMS; MODE OF ACTION; N-TERMINALS; PEPTIDE SEQUENCES; PHARMACEUTICAL APPLICATIONS; POSITIVE CHARGES; STRUCTURAL MODELS; TFE; TRIFLUOROETHANOL;

DICHROISM; ETHANOL; HYDROPHOBICITY; MODEL STRUCTURES; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POLYPEPTIDES;

PEPTIDES;

ESCULENTIN 1B; POLYPEPTIDE ANTIBIOTIC AGENT; TRIFLUOROETHANOL; UNCLASSIFIED DRUG; WATER;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ANTIBACTERIAL ACTIVITY; ANURA; ARTICLE; BACTERIAL MEMBRANE; CIRCULAR DICHROISM; CYTOTOXICITY; DRUG STRUCTURE; EUKARYOTIC CELL; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN FOLDING; SKIN;

AMPHIBIAN PROTEINS; ANIMALS; ANTI-INFECTIVE AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; ANURA; CIRCULAR DICHROISM; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; OLIGOPEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SKIN; SOLUTIONS; STATIC ELECTRICITY; TRIFLUOROETHANOL; WATER;

EID: 84865124549     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.22086     Document Type: Article

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