Accretion of structure in staphylococcal nuclease: An 15N NMR relaxation study

Journal of Molecular Biology

Volumn 260, Issue 4, 1996, Pages 570-587

  Alexandrescu, Andrei T ^a   Jahnke, Wolfgang ^b   Wiltscheck, Ronald ^a   Blommers, Marcel J J ^b  

^a UNIVERSITY OF BASEL   (Switzerland)

^b CIBA GEIGY LTD   (Switzerland)

Author keywords

Chemical shift; Coupling constant; NMR structure; Protein dynamics; Protein folding

Indexed keywords

BACTERIAL ENZYME; NITROGEN 15; NUCLEASE;

ARTICLE; CONTROLLED STUDY; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME STABILITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; STAPHYLOCOCCUS;

BACTERIA (MICROORGANISMS); STAPHYLOCOCCUS;

EID: 0030602880     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0422     Document Type: Article

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