Structure, dynamics and mapping of membrane-binding residues of micelle-bound antimicrobial peptides by natural abundance 13C NMR spectroscopy

Biochimica et Biophysica Acta - Biomembranes

Volumn 1798, Issue 2, 2010, Pages 114-121

  Wang, Guangshun ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

Antimicrobial peptides; Chemical shifts; Dynamics; HSQC wave; Membrane proteins; Membrane binding residues; Micelles; NMR waves

Indexed keywords

ALANINE; ANTIMICROBIAL PEPTIDE GF 17; ANTIMICROBIAL PEPTIDE KR 12; ANTIMICROBIAL PEPTIDE LLAA; ANTIMICROBIAL PEPTIDE RI 10; AUREIN 1.2; PHENYLALANINE; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

ANTIBACTERIAL ACTIVITY; ARTICLE; BACTERIUM CULTURE; CARBON NUCLEAR MAGNETIC RESONANCE; CONTROLLED STUDY; DRUG BINDING SITE; DRUG STRUCTURE; GENE MUTATION; HYDROPHOBICITY; MICELLE; MUTANT; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE;

ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; CARBON ISOTOPES; HUMANS; HYDROPHOBICITY; LIPIDS; MEMBRANES, ARTIFICIAL; MICELLES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; STRUCTURE-ACTIVITY RELATIONSHIP;

AMPHIBIA; BACTERIA (MICROORGANISMS);

EID: 74249106997     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.07.028     Document Type: Article

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