通过蛋白质工程分析氢键与生物特异性

Hydrogen bonding and biological specificity analysed by protein engineering.

作者信息

Fersht A R, Shi J P, Knill-Jones J, Lowe D M, Wilkinson A J, Blow D M, Brick P, Carter P, Waye M M, Winter G

出版信息

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

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.

摘要

通过对酪氨酰 - tRNA合成酶进行蛋白质工程，研究了互补氢键作为生物特异性决定因素的作用。在酶与底物之间删除一个侧链，留下一个未配对、不带电荷的氢键供体或受体，会使结合能仅降低0.5 - 1.5千卡/摩尔。但是存在一个未配对且带电荷的供体或受体会使结合力进一步减弱约3千卡/摩尔。