Asymmetric maltose neopentyl glycol amphiphiles for a membrane protein study: effect of detergent asymmetricity on protein stability
- Title
- Asymmetric maltose neopentyl glycol amphiphiles for a membrane protein study: effect of detergent asymmetricity on protein stability
- Author
- 채필석
- Issue Date
- 2019-01
- Publisher
- Royal Society of Chemistry
- Citation
- Chemical Science, v. 10, NO. 4, Page. 1107-1116
- Abstract
- Maintaining protein stability in an aqueous solution is a prerequisite for protein structural and functional studies, but conventional detergents have increasingly showed limited ability to maintain protein integrity. A representative novel agent, maltose neopentyl glycol-3 (MNG-3), has recently substantially contributed to membrane protein structural studies. Motivated by the popular use of this novel agent, we prepared asymmetric versions of MNG-3 and evaluated these agents with several membrane proteins including two G protein-coupled receptors in this study. We found that some new MNGs were significantly more effective than MNG-3 at preserving protein integrity in the long term, suggesting that these asymmetric MNGs will find a wide use in membrane protein studies. In addition, this is the first study addressing the favorable effect of detergent asymmetric nature on membrane protein stability.
- URI
- https://pubs.rsc.org/en/content/articlelanding/2019/SC/C8SC02560Fhttps://repository.hanyang.ac.kr/handle/20.500.11754/176099
- ISSN
- 2041-6520;2041-6539
- DOI
- 10.1039/c8sc02560f
- Appears in Collections:
- COLLEGE OF ENGINEERING SCIENCES[E](공학대학) > BIONANO ENGINEERING(생명나노공학과) > Articles
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