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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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| Published in: | Nature (London) 1985-03, Vol.314 (6008), p.235-238 |
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| Main Authors: | , , , , , , , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c395t-f27716663d2cbafdfcde53c8031a0427c5743bae16e3d17a7d6a76ec7d83ea2e3 |
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| cites | cdi_FETCH-LOGICAL-c395t-f27716663d2cbafdfcde53c8031a0427c5743bae16e3d17a7d6a76ec7d83ea2e3 |
| container_end_page | 238 |
| container_issue | 6008 |
| container_start_page | 235 |
| container_title | Nature (London) |
| container_volume | 314 |
| creator | 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 |
| description | 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
. |
| doi_str_mv | 10.1038/314235a0 |
| format | article |
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−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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−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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−1
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| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1985-03, Vol.314 (6008), p.235-238 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76043352 |
| source | Nature |
| 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 |
| title | Hydrogen bonding and biological specificity analysed by protein engineering |
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