Article
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 A resolution.
Protein science : a publication of the Protein Society - 1 Jan 2002
Chatani Eri, Hayashi Rikimaru, Moriyama Hideaki, Ueki Tatzuo
Abstract excerpt
The replacement of Phe120 with other hydrophobic residues causes a decrease in the activity and thermal stability in ribonuclease A (RNase A). To explain this, the crystal structures of wild-type RNase A and three mutants--F120A, F120G, and F120W--were analyzed up to a 1.4 A resolution. Although the overall backbone structures of all mutant samples were nearly the same as that of wild-type RNase A, except for the...
Topics
- Animals
- Binding Sites
- Cattle
- Crystallography, X-Ray
- Histidine
- Lysine
- Models, Molecular
- Mutation
- Phenylalanine
- Protein Binding
- Protein Conformation