Hydrogen bonding and biological specificity analysed by protein engineering
Publication in refereed journal


香港中文大学研究人员 ( 现职)

韦妙宜教授 (那打素护理学院)

全文

数位物件识别号 (DOI) http://dx.doi.org/10.1038/314235a0 出版商提供的全文 http://www.nature.com/nature/journal/v314/n6008/abs/314235a0.html

引用次数
Web of Sciencehttp://aims.cuhk.edu.hk/converis/portal/Publication/971WOS source URL
Scopushttp://aims.cuhk.edu.hk/converis/portal/Publication/707Scopus source URL

其它资讯

摘要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.

着者Fersht AR, Shi JP, Knill-Jones J, Lowe DM, Wilkinson AJ, Blow DM, Brick P, Carter P, Waye MM, Winter G
期刊名称Nature
出版年份1985
月份3
日期21
卷号314
期次6008
出版社Nature Publishing Group
页次235 - 238
国际标準期刊号0028-0836
电子国际标準期刊号1476-4687
语言英式英语