par Popot, J-L;Althoff, T;Bagnard, D;Banères, J-L;Bazzacco, P;Billon-Denis, E;Catoire, L J;Champeil, P;Charvolin, D;Cocco, M J;Crémel, G;Dahmane, T;de la Maza, L M;Ebel, C;Gabel, F;Giusti, F;Gohon, Y;Goormaghtigh, Erik 
;Guittet, Emmanuel-Pierre ;Kleinschmidt, J H;Kühlbrandt, W;Le Bon, C;Martinez, K L;Picard, Melanie ;Pucci, B;Sachs, J N;Tribet, Christophe;van Heijenoort, C;Wien, F;Zito, F;Zoonens, M
Référence Annual Review of Biophysics, 40, page (379-408)
Publication Publié, 2011
;Guittet, Emmanuel-Pierre ;Kleinschmidt, J H;Kühlbrandt, W;Le Bon, C;Martinez, K L;Picard, Melanie ;Pucci, B;Sachs, J N;Tribet, Christophe;van Heijenoort, C;Wien, F;Zito, F;Zoonens, MRéférence Annual Review of Biophysics, 40, page (379-408)
Publication Publié, 2011
Article révisé par les pairs
| Résumé : | Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep integral membrane proteins (MPs) water soluble. In this review, we discuss their structure and solution behavior; the way they associate with MPs; and the structure, dynamics, and solution properties of the resulting complexes. All MPs tested to date form water-soluble complexes with APols, and their biochemical stability is in general greatly improved compared with MPs in detergent solutions. The functionality and ligand-binding properties of APol-trapped MPs are reviewed, and the mechanisms by which APols stabilize MPs are discussed. Applications of APols include MP folding and cell-free synthesis, structural studies by NMR, electron microscopy and X-ray diffraction, APol-mediated immobilization of MPs onto solid supports, proteomics, delivery of MPs to preexisting membranes, and vaccine formulation. |
