채필석
2017-03-14T07:10:17Z
2017-03-14T07:10:17Z
2015-07
ANALYTICAL METHODS, v. 7, NO 14, Page. 5808-5813
1759-9660
1759-9679
http://pubs.rsc.org/en/Content/ArticleLanding/2015/AY/C4AY03091E#!divAbstract
http://hdl.handle.net/20.500.11754/26104
Membrane protein manipulation is known to be an extremely challenging task, mainly because of incompatibility between the hydrophobic surface area of proteins and the hydrophilic character of an aqueous medium. To avoid protein degradation resulting from this incompatibility, detergents are used as essential tools in the study of membrane proteins. However, traditional detergents have a limited ability to stabilize the native conformation of membrane proteins. This study introduces a novel tripod amphiphile that can be prepared efficiently from a commercially available compound. The new agent proved effective for the long-term stability of a multi-subunit superassembly, a membrane protein sensitive to denaturation.
This work was supported by the research fund of Hanyang University (HY-2013-N).
en
ROYAL SOC CHEMISTRY
MUSCARINIC ACETYLCHOLINE-RECEPTOR
FACIAL AMPHIPHILES
AQUEOUS-SOLUTIONS
CRYSTAL-STRUCTURE
MNG AMPHIPHILES
GNG AMPHIPHILES
STABILIZATION
SOLUBILIZATION
DETERGENT
CRYSTALLIZATION
Accessible glyco-tripod amphiphiles for membrane protein analysis
Article
14
7
10.1039/c4ay03091e
5808-5813
ANALYTICAL METHODS
Das, Manabendra
Bae, Hyoung Eun
Lee, Ho Jin
Go, Juyeon
Chae, Pil Seok
2015006710
S
GRADUATE SCHOOL[S]
DEPARTMENT OF BIONANOTECHNOLOGY
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