Hydrogen bonding and biological specificity analysed by protein engineering

Nature. 1985 Mar;314(6008):235-8. doi: 10.1038/314235a0.


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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acyl-tRNA Synthetases / metabolism*
  • Chemical Phenomena
  • Chemistry
  • Geobacillus stearothermophilus / enzymology
  • Hydrogen Bonding
  • Kinetics
  • RNA, Transfer, Amino Acyl / metabolism
  • Structure-Activity Relationship
  • Substrate Specificity
  • Thermodynamics
  • Tyrosine-tRNA Ligase / metabolism*
  • Water


  • RNA, Transfer, Amino Acyl
  • Water
  • Amino Acyl-tRNA Synthetases
  • Tyrosine-tRNA Ligase