Hydrogen bonding and biological specificity analysed by protein engineering
| Autor: | Paul Carter, Jian-Ping Shi, J.W. Knill-Jones, Mary M.Y. Waye, Peter Brick, David M. Blow, Denise M. Lowe, Alan R. Fersht, Greg Winter, Anthony J. Wilkinson |
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| Rok vydání: | 1985 |
| Předmět: |
Multidisciplinary
Chemical Phenomena Chemistry Hydrogen bond Stereochemistry Binding energy Water Substrate (chemistry) Hydrogen Bonding Protein engineering RNA Transfer Amino Acyl Acceptor Substrate Specificity Amino Acyl-tRNA Synthetases Geobacillus stearothermophilus Kinetics Structure-Activity Relationship Biological specificity Tyrosine-tRNA Ligase Side chain Thermodynamics Binding site |
| Zdroj: | Nature. 314:235-238 |
| ISSN: | 1476-4687 0028-0836 |
| Popis: | 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 approximately 3 kcal mol-1. |
| Databáze: | OpenAIRE |
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