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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
March 1985
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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.