期刊
NATURE METHODS
卷 7, 期 12, 页码 1003-U90出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH.1526
关键词
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资金
- US National Institutes of Health (NIH) [P01 GM75913, NS28471]
- Lundbeck Foundation
- Danish National Research Council
- European Community [FP7/2007-2013, HEALTH-F4-2007-201924]
- EDICT Consortium
- NIH [GM083118]
- NIH Protein Structure Initiative [U54]
- US National Heart, Lung, and Blood Institute [R21HL087895]
- Texas Norman Hackerman Advanced Research Program [010674-0034-2009]
- Center for Membrane Protein Research
- Texas Tech University Health Sciences Center
- Defence Science and Technology Laboratory
- Lundbeck Foundation [R19-2008-2113, R37-2009-3457] Funding Source: researchfish
The understanding of integral membrane protein (IMP) structure and function is hampered by the difficulty of handling these proteins. Aqueous solubilization, necessary for many types of biophysical analysis, generally requires a detergent to shield the large lipophilic surfaces of native IMPs. Many proteins remain difficult to study owing to a lack of suitable detergents. We introduce a class of amphiphiles, each built around a central quaternary carbon atom derived from neopentyl glycol, with hydrophilic groups derived from maltose. Representatives of this maltose-neopentyl glycol (MNG) amphiphile family show favorable behavior relative to conventional detergents, as manifested in multiple membrane protein systems, leading to enhanced structural stability and successful crystallization. MNG amphiphiles are promising tools for membrane protein science because of the ease with which they may be prepared and the facility with which their structures may be varied.
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