| Literature DB >> 24123610 |
Pil Seok Chae1, Andrew C Kruse, Kamil Gotfryd, Rohini R Rana, Kyung Ho Cho, Søren G F Rasmussen, Hyoung Eun Bae, Richa Chandra, Ulrik Gether, Lan Guan, Brian K Kobilka, Claus J Loland, Bernadette Byrne, Samuel H Gellman.
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.Entities:
Keywords: amphiphiles; membrane proteins; molecular design; protein structures; stabilization
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Year: 2013 PMID: 24123610 PMCID: PMC3947462 DOI: 10.1002/chem.201301423
Source DB: PubMed Journal: Chemistry ISSN: 0947-6539 Impact factor: 5.236