1H-15N NMR dynamic study of an isolated α-helical peptide (1-36)-bacteriorhodopsin reveals the equilibrium helix-coil transitions

Journal of Biomolecular NMR

Volumn 14, Issue 4, 1999, Pages 345-356

  Orekhov, Vladislav Yu ^a,b   Korzhnev, Dmitry M ^a   Diercks, Tammo ^c   Kessler, Horst ^c   Arseniev, Alexander S ^a  

^a SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

^b UNIVERSITY OF GOTHENBURG   (Sweden)

^c TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Alpha helix; Anisotropy; Bacteriorhodopsin; CSA; Hydrogen bond; Random coil; Relaxation

Indexed keywords

AMIDE; BACTERIORHODOPSIN; MEMBRANE PROTEIN; NITROGEN 15; PEPTIDE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANISOTROPY; ARTICLE; HYDROGEN BOND; MATHEMATICAL MODEL; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN STRUCTURE; STATISTICAL ANALYSIS;

EID: 0032884804     PISSN: 09252738     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1008356809071     Document Type: Article

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