His···Asp catalytic dyad of ribonuclease A: Conformational stability of the wild-type, D121N, D121A, and H119A enzymes

Biochemistry

Volumn 37, Issue 51, 1998, Pages 17958-17964

  Quirk, David J ^a   Park, Chiwook ^a   Thompson, James E ^a,b   Raines, Ronald T ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b MERCK RESEARCH LABORATORIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ASPARAGINE; ASPARTIC ACID; HISTIDINE; RIBONUCLEASE A; PANCREATIC RIBONUCLEASE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENTHALPY; ENTROPY; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STABILITY; HYDROGEN BOND; HYDROLYSIS; PKA; PRIORITY JOURNAL; ANIMAL; BINDING SITE; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS;

ALANINE; AMINO ACID SUBSTITUTION; ANIMALS; ASPARTIC ACID; BINDING SITES; CATALYSIS; CATTLE; ENZYME STABILITY; HISTIDINE; HYDROGEN BONDING; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RIBONUCLEASE, PANCREATIC;

EID: 0032558938     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi981688j     Document Type: Article

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