Planchard Noelya, Point Élodie, Dahmane Tassadite, Giusti Fabrice, Renault Marie, Le Bon Christel, Durand Grégory, Milon Alain, Guittet Éric, Zoonens Manuela, Popot Jean-Luc, Catoire Laurent J
Laboratoire de Biologie Physico-Chimique des Protéines Membranaires, Institut de Biologie Physico-Chimique (FRC 550), UMR 7099, CNRS, Université Paris 7, 13 rue Pierre et Marie Curie, 75005, Paris, France.
J Membr Biol. 2014 Oct;247(9-10):827-42. doi: 10.1007/s00232-014-9654-z. Epub 2014 Mar 28.
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.
与去污剂溶液相比，两性分子捕获赋予大多数膜蛋白更高的稳定性，从而促进了溶液状态下膜蛋白的核磁共振研究。这些研究提供了有关蛋白质折叠状态、它们与聚合物的接触区域、动力学、水可及性以及蛋白质结合配体结构的信息。它们受益于两性分子化学结构的多样化以及氘代两性分子的可得性。文中讨论了使用两性分子的优势和限制，并与其他非常规环境（如双分子层和纳米盘）相关的优势和限制进行了比较。
