Membrane-bound dimer structure of a β-hairpin antimicrobial peptide from rotational-echo double-resonance solid-state NMR

Biochemistry

Volumn 45, Issue 27, 2006, Pages 8341-8349

  Mani, R ^a   Tang, M ^a   Wu, X ^a   Buffy, J J ^a,d   Waring, A J ^b   Sherman, M A ^c   Hong, M ^a  

^a IOWA STATE UNIVERSITY   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c CITY OF HOPE NATIONAL MEDICAL CENTER   (United States)

^d UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMERS; ENZYMES; HYDROGEN BONDS; MICELLES; OLIGOMERS; STABILITY;

AMPHIPATHIC LIPID BILAYER; ANTIMICROBIAL PEPTIDE; INTERMOLECULAR INTERFACE; LIPID BILAYERS; ROTATIONAL-ECHO DOUBLE-RESONANCE (REDOR);

NUCLEAR MAGNETIC RESONANCE;

CARBON 13; DIMER; FLUORINE; HYDROGEN; MEMBRANE PROTEIN; NITROGEN 15; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEGRIN 1; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ARTICLE; HYDROGEN BOND; LIPID BILAYER; MEMBRANE BINDING; MICELLE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; ROTATIONAL ECHO DOUBLE RESONANCE SOLID STATE NUCLEAR MAGNETIC RESONANCE;

ANTIMICROBIAL CATIONIC PEPTIDES; DIMERIZATION; HYDROGEN BONDING; LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; PHOSPHATIDYLCHOLINES; PROTEIN STRUCTURE, SECONDARY; PROTEINS;

EID: 33745855891     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060305b     Document Type: Article

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