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 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.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D001411:Geobacillus stearothermophilus / Q000201:enzymology; D006860:Hydrogen Bonding; D007700:Kinetics; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013816:Thermodynamics; D014448:Tyrosine-tRNA Ligase / Q000378:metabolism*; D014867:Water
D012346:RNA, Transfer, Amino Acyl; D014867:Water; D000604:Amino Acyl-tRNA Synthetases; D014448:Tyrosine-tRNA Ligase