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- W2805129007 abstract "Folding membrane proteins (MPs) in vitro is important from both practical and theoretical points of view. Amphipols (APols) have emerged as an interesting medium in which to fold MPs. Both α-helical and β-barrel MPs are amenable to folding in APols, using simple procedures and achieving high yields. All APols hitherto tested (A8-35, sulfonated APols, non-ionic APols) have proven to provide a medium favorable to MP folding. From a practical point of view, the approach is particularly interesting when applied to MPs that have been produced in large amounts in inclusion bodies, from which they can be recovered only under a denatured state. The resulting MP/APol complexes can be used as such or the protein transferred to other media more appropriate to a given type of experiment (e.g. to lipidic mesophases for crystallization). From a theoretical point of view, the observation that MPs can fold very efficiently in a medium so different from a lipid bilayer raises interesting questions about the forces that determine the final fold." @default.
- W2805129007 created "2018-06-13" @default.
- W2805129007 creator A5043521883 @default.
- W2805129007 date "2018-01-01" @default.
- W2805129007 modified "2023-09-27" @default.
- W2805129007 title "Amphipol-Assisted Folding of Membrane Proteins" @default.
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- W2805129007 doi "https://doi.org/10.1007/978-3-319-73148-3_6" @default.
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