152 0

Novel Tripod Amphiphiles for Membrane Protein Analysis

Title
Novel Tripod Amphiphiles for Membrane Protein Analysis
Author
채필석
Keywords
amphiphiles; membrane proteins; molecular design; protein structures; stabilization
Issue Date
2013-11
Publisher
John Wiley & Sons Ltd.
Citation
Chemistry - A European Journal, v. 19, NO. 46, Page. 15645-15651
Abstract
Integral membrane proteins play central roles in controlling the flow of information and molecules across membranes. Our understanding of membrane protein structures and functions, however, is seriously limited, mainly due to difficulties in handling and analysing these proteins in aqueous solution. The use of a detergent or other amphipathic agents is required to overcome the intrinsic incompatibility between the large lipophilic surfaces displayed by the membrane proteins in their native forms and the polar solvent molecules. Here, we introduce new tripod amphiphiles displaying favourable behaviours toward several membrane protein systems, leading to an enhanced protein solubilisation and stabilisation compared to both conventional detergents and previously described tripod amphiphiles.
URI
https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/chem.201301423https://repository.hanyang.ac.kr/handle/20.500.11754/176146
ISSN
0947-6539;1521-3765
DOI
10.1002/chem.201301423
Appears in Collections:
COLLEGE OF ENGINEERING SCIENCES[E](공학대학) > BIONANO ENGINEERING(생명나노공학과) > Articles
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE