Thermodynamics of the coil-α-helix transition of amphipathic peptides in a membrane environment: The role of vesicle curvature

Biophysical Chemistry

Volumn 96, Issue 2-3, 2002, Pages 191-201

  Wieprecht, Torsten ^a   Beyermann, Michael ^b   Seelig, Joachim ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

Author keywords

Amphipathic peptide; Helix coil transition; Magainin; Peptide membrane interaction; Titration calorimetry

Indexed keywords

AMINO ACID; PEPTIDE DERIVATIVE; ANTIMICROBIAL CATIONIC PEPTIDE; LIPOSOME; MAGAININ 2 PEPTIDE, XENOPUS; MEMBRANE PROTEIN; PEPTIDE; PHOSPHOLIPID; XENOPUS PROTEIN;

ALPHA HELIX; ARTICLE; BILAYER MEMBRANE; CORRELATION ANALYSIS; ENANTIOMER; ENERGY TRANSFER; ENTHALPY; ENTROPY; MEMBRANE BINDING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; THERMODYNAMICS; ANIMAL; BIOLOGICAL MODEL; CALORIMETRY; CHEMISTRY; DRUG EFFECT; METABOLISM; PROTEIN SECONDARY STRUCTURE;

ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; CALORIMETRY; LIPOSOMES; MEMBRANE PROTEINS; MODELS, BIOLOGICAL; PEPTIDES; PHOSPHOLIPIDS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS; XENOPUS PROTEINS;

EID: 0037007486     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00025-X     Document Type: Article

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