Three-Dimensional Solid-State NMR Spectroscopy Is Essential for Resolution of Resonances from In-Plane Residues in Uniformly 15 N-Labeled Helical Membrane Proteins in Oriented Lipid Bilayers

Journal of Magnetic Resonance

Volumn 144, Issue 1, 2000, Pages 156-161

  Marassi, Francesca M ^a   Ma, Che ^b   Gesell, Jennifer J ^b   Opella, Stanley J ^b  

^a WISTAR INSTITUTE   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Magainin; Membrane protein; PISEMA; Protein structure; Solid state NMR

Indexed keywords

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

ANIMAL; ARTICLE; CHEMISTRY; HUMAN IMMUNODEFICIENCY VIRUS 1; LIPID BILAYER; METHODOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN SECONDARY STRUCTURE;

ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; GENE PRODUCTS, VPU; HIV-1; LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; NITROGEN ISOTOPES; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; XENOPUS PROTEINS;

EID: 0034183383     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.2000.2036     Document Type: Editorial

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