Hydrogen bonding in enzymatic catalysis analysed by protein engineering
- 1 August 1985
- journal article
- Published by Springer Nature in Nature
- Vol. 316 (6029), 656-657
- https://doi.org/10.1038/316656a0
Abstract
No abstract availableKeywords
This publication has 6 references indexed in Scilit:
- Hydrogen bonding and biological specificity analysed by protein engineeringNature, 1985
- The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)Cell, 1984
- A large increase in enzyme–substrate affinity by protein engineeringNature, 1984
- Deletion mutagenesis using an ‘M13 splint’: the N-terminal structural domain of tyrosyl-tRNA synthetase (B. stearothermophilus) catalyses the formation of tyrosyl adenylate.The EMBO Journal, 1983
- Ligand binding and enzymic catalysis coupled through subunits in tyrosyl-tRNA synthetaseBiochemistry, 1975
- Molecular Architecture and Biological ReactionsPublished by American Chemical Society (ACS) ,1946