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A class of rigid linker-bearing glucosides for membrane protein structural study

Title
A class of rigid linker-bearing glucosides for membrane protein structural study
Author
채필석
Keywords
MUSCARINIC ACETYLCHOLINE-RECEPTOR; GLYCOL GNG AMPHIPHILES; COUPLED RECEPTORS; CRYSTAL-STRUCTURE; MNG AMPHIPHILES; STABILIZATION; SOLUBILIZATION; CRYSTALLIZATION; DETERGENTS; STABILITY
Issue Date
2016-02
Publisher
ROYAL SOC CHEMISTRY
Citation
CHEMICAL SCIENCE, v. 7, NO 3, Page. 1933-1939
Abstract
Membrane proteins are amphipathic bio-macromolecules incompatible with the polar environments of aqueous media. Conventional detergents encapsulate the hydrophobic surfaces of membrane proteins allowing them to exist in aqueous solution. Membrane proteins stabilized by detergent micelles are used for structural and functional analysis. Despite the availability of a large number of detergents, only a few agents are sufficiently effective at maintaining the integrity of membrane proteins to allow successful crystallization. In the present study, we describe a novel class of synthetic amphiphiles with a branched tail group and a triglucoside head group. These head and tail groups were connected via an amide or ether linkage by using a tris(hydroxylmethyl) aminomethane (TRIS) or neopentyl glycol (NPG) linker to produce TRIS-derived triglucosides (TDTs) and NPG-derived triglucosides (NDTs), respectively. Members of this class conferred enhanced stability on target membrane proteins compared to conventional detergents. Because of straightforward synthesis of the novel agents and their favourable effects on a range of membrane proteins, these agents should be of wide applicability to membrane protein science.
URI
http://pubs.rsc.org/en/content/articlelanding/2016/sc/c5sc02900g#!divAbstracthttp://hdl.handle.net/20.500.11754/31853
ISSN
2041-6520; 2041-6539
DOI
10.1039/c5sc02900g
Appears in Collections:
GRADUATE SCHOOL[S](대학원) > BIONANOTECHNOLOGY(바이오나노학과) > Articles
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