| Literature DB >> 21545287 |
J-L Popot1, T Althoff, D Bagnard, J-L Banères, P Bazzacco, E Billon-Denis, L J Catoire, P Champeil, D Charvolin, M J Cocco, G Crémel, T Dahmane, L M de la Maza, C Ebel, F Gabel, F Giusti, Y Gohon, E Goormaghtigh, E Guittet, J H Kleinschmidt, W Kühlbrandt, C Le Bon, K L Martinez, M Picard, B Pucci, J N Sachs, C Tribet, C van Heijenoort, F Wien, F Zito, M Zoonens.
Abstract
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.Entities:
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Year: 2011 PMID： 21545287 DOI： 10.1146/annurev-biophys-042910-155219
Source DB: PubMed Journal: Annu Rev Biophys ISSN： 1936-122X Impact factor: 12.981