Hydrogen bonding and biological specificity analysed by protein engineering View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1985-03

AUTHORS

Alan R. Fersht, Jian-Ping Shi, Jack Knill-Jones, Denise M. Lowe, Anthony J. Wilkinson, David M. Blow, Peter Brick, Paul Carter, Mary M. Y. Waye, Greg Winter

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. More... »

PAGES

235-238

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/314235a0

DOI

http://dx.doi.org/10.1038/314235a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1053524488

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/3845322


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