Please use this identifier to cite or link to this item:
|Title:||Evaluating the role of puckering and fluorine atom in stability and folding of fluoroproline containing proteins||Authors:||Nadarajan, Saravanan Prabhu
|Issue Date:||2017||Source:||Nadarajan, S. P., Deepankumar, K., Seo, J.-H., & Yun, H. (2017). Evaluating the role of puckering and fluorine atom in stability and folding of fluoroproline containing proteins. Biotechnology and Bioprocess Engineering, 22(5), 504-511.||Series/Report no.:||Biotechnology and Bioprocess Engineering||Abstract:||In the past decade, numerous studies have been reported that the residue specific incorporation of fluorine containing analogs into protein can enhance the stability of protein. On the other hand, the incorporation of fluoroproline can enhance both stability and refolding rate of recombinant proteins. The objective of this study was to determine the reason behind the enhanced stability and refolding rate of protein by comparing GFP variants containing fluoroproline or hydroxyproline. The fluorine atom of 4-fluoroproline played a significant role in enhancing stability, and Cγ-endo puckering property of (4S)-4-fluoroproline and (4S)-4-hydroxyproline plays a key role in enhancing protein refolding rate.||URI:||https://hdl.handle.net/10356/86479
|ISSN:||1226-8372||DOI:||http://dx.doi.org/10.1007/s12257-017-0257-2||Rights:||© 2017 The Korean Society for Biotechnology and Bioengineering and Springer||Fulltext Permission:||none||Fulltext Availability:||No Fulltext|
|Appears in Collections:||MSE Journal Articles|
Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.