Characterization of the motion of membrane proteins using high-speed atomic force microscopy

Abstract : For cells to function properly, membrane proteins must be able to diffuse within biological membranes. The functions of these membrane proteins depend on their position and also on protein-protein and protein-lipid interactions. However, so far, it has not been possible to study simultaneously the structure and dynamics of biological membranes. Here, we show that the motion of unlabelled membrane proteins can be characterized using high-speed atomic force microscopy. We find that the molecules of outer membrane protein F (OmpF) are widely distributed in the membrane as a result of diffusion-limited aggregation, and while the overall protein motion scales roughly with the local density of proteins in the membrane, individual protein molecules can also diffuse freely or become trapped by protein-protein interactions. Using these measurements, and the results of molecular dynamics simulations, we determine an interaction potential map and an interaction pathway for a membrane protein, which should provide new insights into the connection between the structures of individual proteins and the structures and dynamics of supramolecular membranes.
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Article dans une revue
Nature Nanotechnology, Nature Publishing Group, 2012, pp.525-529. 〈http://www.nature.com/nnano/journal/v7/n8/full/nnano.2012.109.html〉. 〈10.1038/nnano.2012.109〉
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http://www.hal.inserm.fr/inserm-01363192
Contributeur : U1006 Aix-Marseille Université <>
Soumis le : vendredi 9 septembre 2016 - 14:32:36
Dernière modification le : mardi 17 avril 2018 - 17:52:01
Document(s) archivé(s) le : samedi 10 décembre 2016 - 13:32:14

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Ignacio Casuso, Jonathan Khao, Mohamed Chami, Perrine Paul-Gilloteaux, Mohamed Husain, et al.. Characterization of the motion of membrane proteins using high-speed atomic force microscopy. Nature Nanotechnology, Nature Publishing Group, 2012, pp.525-529. 〈http://www.nature.com/nnano/journal/v7/n8/full/nnano.2012.109.html〉. 〈10.1038/nnano.2012.109〉. 〈inserm-01363192〉

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