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Article
Nature 314, 235-238 (21 March 1985) | doi:10.1038/314235a0; Received 18 December 1984; Accepted 12 February 1985
Hydrogen bonding and biological specificity analysed by protein engineering
Alan R. Fersht*, Jian-Ping Shi*, Jack Knill-Jones*, Denise M. Lowe*, Anthony J. Wilkinson*, David M. Blow†, Peter Brick†, Paul Carter‡, Mary M. Y. Waye‡ & Greg Winter‡
- *, Departments of Chemistry and †Physics, Imperial College of Science and Technology, London SW7 2AY, UK
- ‡MRC Laboratory of Molecular Biology, MRC Centre, Hills Road, Cambridge CB2 2QH, UK
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.
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