Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures

Journal of Molecular Biology

Volumn 268, Issue 1, 1997, Pages 170-184

  Gillespie, Joel R ^a   Shortle, David ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Folding intermediates; Hydrophobic interactions; Protein folding; Spin labeling

Indexed keywords

AMIDE; NUCLEASE;

ARTICLE; CALCULATION; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME STRUCTURE; GEOMETRY; HYDROGEN BOND; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; SPIN LABELING; STAPHYLOCOCCUS;

EID: 0031585992     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.0953     Document Type: Article

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