Article
A thermoresistant mutant of ribonuclease T1 having three disulfide bonds.
Protein engineering - 1 Apr 1990
Nishikawa S, Adiwinata J, Morioka H, Fujimura T, Tanaka T, Uesugi S, Hakoshima T, Tomita K, Nakagawa S, Ikehara M
Abstract excerpt
Molecular-dynamic calculations predict that, if Tyr24 and Asn84 are each replaced by a Cys residue, it should be possible to form a third disulfide bond in ribonuclease T1 (RNase T1) between these residues, with only minimal conformational changes at the catalytic site. The gene encoding such a m...
Topics
- Base Sequence
- Chemical Phenomena
- Chemistry
- Circular Dichroism
- Disulfides
- Electrophoresis, Polyacrylamide Gel
- Exoribonucleases
- Gene Expression Regulation
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Temperature