Analysis of long-range interactions in a model denatured state of staphylococcal nuclease based on correlated changes in backbone dynamics

Protein Science

Volumn 8, Issue 5, 1999, Pages 991-1000

  Sinclair, James F ^a   Shortle, David ^a  

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

Author keywords

15N NMR relaxation; Denatured state; Protein folding; Sodium perchlorate; Staphylococcal nuclease

Indexed keywords

BACTERIAL ENZYME; NUCLEASE; SODIUM PERCHLORATE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME DENATURATION; HYDROGEN BOND; MOLECULAR INTERACTION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN INTERACTION; PROTEIN STRUCTURE; STAPHYLOCOCCUS;

BACTERIA (MICROORGANISMS); STAPHYLOCOCCUS;

EID: 0032948128     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.5.991     Document Type: Article

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