Hydrogen bonding and biological specificity analysed by protein engineering

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...

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Bibliographic Details
Published in:Nature (London) 1985-03, Vol.314 (6008), p.235-238
Main Authors: Fersht, Alan R, Shi, Jian-Ping, Knill-Jones, Jack, Lowe, Denise M, Wilkinson, Anthony J, Blow, David M, Brick, Peter, Carter, Paul, Waye, Mary M. Y, Winter, Greg
Format: Article
Language:English
Subjects:
Amino Acyl-tRNA Synthetases - metabolism
Analytical, structural and metabolic biochemistry
Bacillus stearothermophilus
Biological and medical sciences
Chemical Phenomena
Chemistry
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Geobacillus stearothermophilus - enzymology
Humanities and Social Sciences
Hydrogen Bonding
hydrogen bonds
Kinetics
Ligases
multidisciplinary
RNA, Transfer, Amino Acyl - metabolism
Science
Science (multidisciplinary)
Structure-Activity Relationship
Substrate Specificity
Thermodynamics
tryrosyl-tRNA synthetase
Tyrosine-tRNA Ligase - metabolism
Water
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Summary: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 .
ISSN:0028-0836
1476-4687
DOI:10.1038/314235a0