Hydrogen bonding and biological specificity analysed by protein engineering
Open Access
- 1 March 1985
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 314 (6008), 235-238
- https://doi.org/10.1038/314235a0
Abstract
The role of complementary hydrogen bonding as a determinant of biological specificity has been examined by protein engineering of the tyrosyl-tRNA synthetase. Deletion of a side chain between enzyme and substrate to leave an unpaired, uncharged hydrogen-bond donor or acceptor weakens binding energy by only 0.5–1.5 kcal mol−1. But the presence of an unpaired and charged donor or acceptor weakens binding by a further ∼ 3 kcal mol−1.This publication has 19 references indexed in Scilit:
- Analysis of Enzyme Structure and Activity by Protein EngineeringAngewandte Chemie International Edition in English, 1984
- A large increase in enzyme–substrate affinity by protein engineeringNature, 1984
- Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutationBiochemistry, 1983
- Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP bindingNature, 1982
- Tyrosyl-tRNA synthetase forms a mononucleotide-binding foldJournal of Molecular Biology, 1982
- Amino acid activation in crystalline tyrosyl-tRNA synthetase from Bacillus stearothermophilusJournal of Molecular Biology, 1981
- Binding of tyrosine, adenosine triphosphate and analogues to crystalline tyrosyl transfer RNA synthetaseJournal of Molecular Biology, 1978
- Demonstration of two reaction pathways for the aminoacylation of tRNA. Application of the pulsed quenched flow techniqueBiochemistry, 1975
- Hydrogen Bonds between Model Peptide Groups in SolutionJournal of the American Chemical Society, 1962
- Some Factors in the Interpretation of Protein DenaturationAdvances in protein chemistry, 1959