Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease a as revealed by crystallographic study of three Phe 120 mutants at 1.4 Å resolution

Protein Science

Volumn 11, Issue 1, 2002, Pages 72-81

  Chatani, Eri ^a   Hayashi, Rikimaru ^a   Moriyama, Hideaki ^b   Ueki, Tatzuo ^b  

^a KYOTO UNIVERSITY   (Japan)

^b JAPAN SYNCHROTRON RADIATION RESEARCH INSTITUTE   (Japan)

Author keywords

Accessible surface area; Active site; Crystal structure; His119; Ribonuclease A; Thermal stability

Indexed keywords

PANCREATIC RIBONUCLEASE; PHENYLALANINE;

ARTICLE; BINDING SITE; CATTLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLIZATION; CRYSTALLOGRAPHY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME STABILITY; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; STEREOCHEMISTRY; THERMOSTABILITY;

ANIMALS; BINDING SITES; CATTLE; CRYSTALLOGRAPHY, X-RAY; HISTIDINE; LYSINE; MODELS, MOLECULAR; MUTATION; PHENYLALANINE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RIBONUCLEASE, PANCREATIC; SUBSTRATE SPECIFICITY; TEMPERATURE; THERMODYNAMICS;

BOS TAURUS; BOVINAE;

EID: 0036137008     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.ps.31102     Document Type: Article

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