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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
Keywords
CRYSTAL-STRUCTURE; BETA(2)-ADRENERGIC RECEPTOR; ALLOSTERIC MODULATION; SOLUBILIZATION; STABILIZATION; INSIGHTS; BINDING; CRYSTALLIZATION; AMPHIPOLS; ANALOGS
Issue Date
2019-02
Publisher
ROYAL SOC CHEMISTRY
Citation
CHEMICAL SCIENCE, v. 10, Issue 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/C8SC02560F#!divAbstracthttp://repository.hanyang.ac.kr/handle/20.500.11754/103994
ISSN
2041-6520; 2041-6539
DOI
10.1039/c8sc02560f
Appears in Collections:
GRADUATE SCHOOL[S](대학원) > BIONANOTECHNOLOGY(바이오나노학과) > Articles
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