Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease A as revealed by crystallographic study of three Phe120 mutants at 1.4 Å resolution-Reference-Cited by-同舟云学术

Conformational strictness required for maximum activity and stability of bovine pancreatic ribonuclease A as revealed by crystallographic study of three Phe120 mutants at 1.4 Å resolution

Published:2009-04-13 Issue:1 Volume:11 Page:72-81
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Chatani Eri,Hayashi Rikimaru,Moriyama Hideaki,Ueki Tatzuo

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference40 articles.

1. Evidence on the existence of a purine ligand-induced conformational change in the active site of bovine pancreatic ribonuclease A studied by proton nuclear magnetic resonance spectroscopy;Arus;Biochemistry,1982

2. Reverse transphosphorylation by ribonuclease A needs an intact P2-binding site: Point mutations at Lys-7 and Arg-10 alter the catalytic properties of the enzyme;Boix;J. Biol. Chem.,1994

3. The active site of ribonuclease A from the crystallographic studies of ribonuclease-A-inhibitor complexes;Borkakoti;Eur. J. Biochem.,1983

4. Ribonuclease A: Least-squares refinement of the structure at 1.45 Å resolution;Borkakoti;Acta Crystallogr. B,1982

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