The use of amphipols for solution NMR studies of membrane proteins: advantages and constraints as compared to other solubilizing media. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Membrane Biology Année : 2014

The use of amphipols for solution NMR studies of membrane proteins: advantages and constraints as compared to other solubilizing media.

Fabrice Giusti
Christel Le Bon
Manuela Zoonens

Résumé

Solution-state nuclear magnetic resonance studies of membrane proteins are facilitated by the increased stability that trapping with amphipols confers to most of them as compared to detergent solutions. They have yielded information on the state of folding of the proteins, their areas of contact with the polymer, their dynamics, water accessibility, and the structure of protein-bound ligands. They benefit from the diversification of amphipol chemical structures and the availability of deuterated amphipols. The advantages and constraints of working with amphipols are discussed and compared to those associated with other non-conventional environments, such as bicelles and nanodiscs.
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Dates et versions

hal-03011599 , version 1 (18-11-2020)

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Noelya Planchard, Elodie Point, Tassadite Dahmane, Fabrice Giusti, Marie Renault, et al.. The use of amphipols for solution NMR studies of membrane proteins: advantages and constraints as compared to other solubilizing media.. Journal of Membrane Biology, 2014, 247 (9-10), pp.827-842. ⟨10.1007/s00232-014-9654-z⟩. ⟨hal-03011599⟩
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