Sensitivity of NMR residual dipolar couplings to perturbations in folded and denatured staphylococcal nuclease

Biochemistry

Volumn 44, Issue 17, 2005, Pages 6392-6403

  Sallum, Christine O ^a   Martel, David M ^a   Fournier, Robert S ^a   Matousek, William M ^a   Alexandrescu, Andrei T ^a  

^a UNIVERSITY OF CONNECTICUT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CORRELATION METHODS; NUCLEAR MAGNETIC RESONANCE; PERTURBATION TECHNIQUES; POLYPEPTIDES; PROTEINS; SENSITIVITY ANALYSIS;

NUCLEASE; RESIDUAL DIPOLAR COUPLINGS (RDC); STAPHYLOCOCCAL;

ENZYMES;

BACTERIAL ENZYME; NUCLEASE; POLYPEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; CORRELATION ANALYSIS; DENATURATION; ENZYME STRUCTURE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; STAPHYLOCOCCUS;

ANISOTROPY; BACTERIOPHAGE PF1; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; ESCHERICHIA COLI PROTEINS; GENES, SUPPRESSOR; LINEAR MODELS; MICROCOCCAL NUCLEASE; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS;

EID: 17844390105     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0473410     Document Type: Article

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