Main-chain dynamics of a partially folded protein: 15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol

Journal of Molecular Biology

Volumn 257, Issue 3, 1996, Pages 669-683

  Buck, Matthias ^a,b   Schwalbe, Harald ^a   Dobson, Christopher M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b HARVARD UNIVERSITY   (United States)

Author keywords

15N NMR; Disulphides; Order parameters; Secondary structure; TFE

Indexed keywords

DISULFIDE; LYSOZYME; POLYPEPTIDE; TRIFLUOROETHANOL;

ARTICLE; HEN; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

EID: 0029967685     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0193     Document Type: Article

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