| Literature DB >> 3845322 |
A R Fersht, J P Shi, J Knill-Jones, D M Lowe, A J Wilkinson, D M Blow, P Brick, P Carter, M M Waye, G Winter.
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 approximately 3 kcal mol-1.Entities:
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Year: 1985 PMID： 3845322 DOI： 10.1038/314235a0
Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962