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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acyl-tRNA Synthetases / metabolism*
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Chemical Phenomena
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Chemistry
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Geobacillus stearothermophilus / enzymology
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Hydrogen Bonding
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Kinetics
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RNA, Transfer, Amino Acyl / metabolism
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Structure-Activity Relationship
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Substrate Specificity
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Thermodynamics
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Tyrosine-tRNA Ligase / metabolism*
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Water
Substances
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RNA, Transfer, Amino Acyl
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Water
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Amino Acyl-tRNA Synthetases
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Tyrosine-tRNA Ligase