Accessible glyco-tripod amphiphiles for membrane protein analysis

Title
Accessible glyco-tripod amphiphiles for membrane protein analysis
Authors
채필석
Keywords
MUSCARINIC ACETYLCHOLINE-RECEPTOR; FACIAL AMPHIPHILES; AQUEOUS-SOLUTIONS; CRYSTAL-STRUCTURE; MNG AMPHIPHILES; GNG AMPHIPHILES; STABILIZATION; SOLUBILIZATION; DETERGENT; CRYSTALLIZATION
Issue Date
2015-07
Publisher
ROYAL SOC CHEMISTRY
Citation
ANALYTICAL METHODS, v. 7, NO 14, Page. 5808-5813
Abstract
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.
URI
http://pubs.rsc.org/en/Content/ArticleLanding/2015/AY/C4AY03091E#!divAbstracthttp://hdl.handle.net/20.500.11754/26104
ISSN
1759-9660; 1759-9679
DOI
http://dx.doi.org/10.1039/c4ay03091e
Appears in Collections:
GRADUATE SCHOOL[S](대학원) > BIONANOTECHNOLOGY(바이오나노학과) > Articles
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