Side-chain conformations in an unfolded protein: (χ1) distributions in denatured hen lysozyme determined by heteronuclear 13C, 15N NMR spectroscopy

Journal of Molecular Biology

Volumn 288, Issue 4, 1999, Pages 705-723

  Hennig, Mirko ^a   Bermel, Wolfgang ^c   Spencer, Andrew ^b,d   Dobson, Christopher M ^b   Smith, Lorna J ^b   Schwalbe, Harald ^a  

^a GOETHE UNIVERSITY   (Germany)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c Bruker Analytik GmbH   (Germany)

^d INSTITUTE OF FOOD RESEARCH   (United Kingdom)

Author keywords

( 1) side chain conformations; Denatured proteins; Heteronuclear NMR; Random coil model; Scalar coupling constants

Indexed keywords

CARBON 13; LEUCINE; LYSOZYME; METHIONINE; NITROGEN 15; THREONINE;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CONTROLLED STUDY; HYDROPHOBICITY; ISOTOPE LABELING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN INTERACTION; STATISTICAL MODEL; STEREOSPECIFICITY;

EID: 0032967963     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2722     Document Type: Article

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