Characterization of Conformational Preferences in a Partly Folded Protein by Heteronuclear NMR Spectroscopy: Assignment and Secondary Structure Analysis of Hen Egg-White Lysozyme in Trifluoroethanol

Biochemistry

Volumn 34, Issue 40, 1995, Pages 13219-13232

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

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

EGG WHITE; LYSOZYME; TRIFLUOROETHANOL;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; STRUCTURE ANALYSIS;

AMIDES; AMINO ACID SEQUENCE; ANIMAL; ASPERGILLUS NIGER; CHICKENS; EGG WHITE; HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR SEQUENCE DATA; MURAMIDASE; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SOLVENTS; SUPPORT, NON-U.S. GOV'T; TRIFLUOROETHANOL;

ANIMALIA;

EID: 0028882136     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi00040a038     Document Type: Article

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