Effects of denaturants and substitutions of hydrophobic residues on backbone dynamics of denatured staphylococcal nuclease

Protein Science

Volumn 12, Issue 7, 2003, Pages 1530-1537

  Ohnishi, Satoshi ^a   Shortle, David ^a  

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

Author keywords

Backbone dynamics; Denatured proteins; Hydrophobic interaction; NMR spin relaxation; Urea

Indexed keywords

BACTERIAL ENZYME; CARBOXYL GROUP; NUCLEASE; UREA;

ARTICLE; HYDROPHOBICITY; MOLECULAR DYNAMICS; NUCLEAR OVERHAUSER EFFECT; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; PROTON TRANSPORT;

AMINO ACID SUBSTITUTION; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; MAGNETIC RESONANCE SPECTROSCOPY; MICROCOCCAL NUCLEASE; PROTEIN CONFORMATION; PROTEIN DENATURATION; UREA;

BACTERIA (MICROORGANISMS);

EID: 0037633964     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0306403     Document Type: Article

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