期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 19, 期 46, 页码 15645-15651出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201301423
关键词
amphiphiles; membrane proteins; molecular design; protein structures; stabilization
资金
- National Research Foundation of Korea (NRF)
- Korea government (MSIP) [2008-0061891, 2012R1A1A1040964]
- NIH [P01 GM75913, NS28471, R01 GM95538, R21 HL087895]
- European Community [HEALTH-F4-2007-201924]
- EDICT Consortium
- Danish National Research Council
- Lundbeck Foundation
- Defence, Science and Technology Laboratories (DSTL), Porton Down, UK
- Lundbeck Foundation [R37-2009-3457] Funding Source: researchfish
- National Research Foundation of Korea [2008-0061891] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1158085] Funding Source: National Science Foundation
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.
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