Membrane-disruptive abilities of β-hairpin antimicrobial peptides correlate with conformation and activity: A 31P and 1H NMR study

Biochimica et Biophysica Acta - Biomembranes

Volumn 1716, Issue 1, 2005, Pages 11-18

  Mani, Rajeswari ^a   Waring, Alan J ^b   Lehrer, Robert I ^b   Hong, Mei ^a  

^a IOWA STATE UNIVERSITY   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

31P solid state NMR; Antimicrobial peptide; Conformation; Membrane disorder; PG 1; Solution NMR

Indexed keywords

PROTEGRIN;

ANTIMICROBIAL ACTIVITY; ARTICLE; CATION TRANSPORT; GENE MUTATION; MEMBRANE TRANSPORT; PHOSPHORUS NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN LIPID INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; WILD TYPE;

AMINO ACID SEQUENCE; ANIONS; ANTIMICROBIAL CATIONIC PEPTIDES; CATIONS; CELL MEMBRANE; ESCHERICHIA COLI; GLASS; LIPID BILAYERS; LIPIDS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANES, ARTIFICIAL; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDES; PHOSPHORUS RADIOISOTOPES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 25644459933     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2005.08.008     Document Type: Article

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