We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins.
- Authors
Pil Seok Chae; Rasmussen, Søren G F; Rana, Rohini R.; Gotfryd, Kamil; Chandra, Richa; Goren, Michael A.; Kruse, Andrew C.; Nurva, Shailika; Loland, Claus J.; Pierre, Yves; Drew, David; Popot, Jean-Luc; Picot, Daniel; Fox, Brian G.; Lan Guan; Gether, Ulrik; Byrne, Bernadette; Kobilka, Brian; Gellman, Samuel H.
- Abstract
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.
- Publication
Nature Methods, 2010, Vol 7, Issue 12, p1003
- ISSN
1548-7091
- Publication type
Academic Journal
- DOI
10.1038/nmeth.1526