Orientations of helical peptides in membrane bilayers by solid state NMR spectroscopy

Solid State Nuclear Magnetic Resonance

Volumn 7, Issue 3, 1996, Pages 185-191

  Bechinger, B ^a,e   Gierasch, L M ^b   Montal, M ^c   Zasloff, M ^d   Opella, S J ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF MASSACHUSETTS   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d Genaera Corporation   (United States)

^e MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Chemical shift anisotropy; Membrane bilayer; Membrane peptide; Oriented sample; Solid state NMR spectroscopy

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; MAGAININ 2 PEPTIDE, XENOPUS; MEMBRANE PROTEIN; NITROGEN; PEPTIDE; XENOPUS PROTEIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMISTRY; FROGS AND TOADS; LIPID BILAYER; METHODOLOGY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHYSICAL CHEMISTRY; PROTEIN SECONDARY STRUCTURE; TORPEDO;

AMINO ACID SEQUENCE; ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; ANURA; CHEMISTRY, PHYSICAL; LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; TORPEDO; XENOPUS PROTEINS;

ANISOTROPY; LIPIDS; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

CHEMICAL SHIFT ANISOTROPY; HELICAL PEPTIDES; MEMBRANE BILAYER; ORIENTED SAMPLE;

PROTEINS;

EID: 0030300090     PISSN: 09262040     EISSN: None     Source Type: Journal    
DOI: 10.1016/0926-2040(95)01224-9     Document Type: Article

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