Proteoliposomes - a system to study membrane proteins under buffer gradients by cryo-EM

Sejwal, Kushal and Chami, Mohamed and Baumgartner, Paul and Kowal, Julia and Mueller, Shirley A. and Stahlberg, Henning. (2017) Proteoliposomes - a system to study membrane proteins under buffer gradients by cryo-EM. Nanotechnology Reviews, 6 (1). pp. 57-74.

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Official URL: https://edoc.unibas.ch/78620/

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Membrane proteins are vital to life and major therapeutic targets. Yet, understanding how they function is limited by a lack of structural information. In biological cells, membrane proteins reside in lipidic membranes and typically experience different buffer conditions on both sides of the membrane or even electric potentials and transmembrane gradients across the membranes. Proteoliposomes, which are lipidic vesicles filled with reconstituted membrane proteins, provide an ideal model system for structural and functional studies of membrane proteins under conditions that mimic nature to a certain degree. We discuss methods for the formation of liposomes and proteoliposomes, their imaging by cryo-electron microscopy, and the structural analysis of proteins present in their bilayer. We suggest the formation of ordered arrays akin to weakly ordered two-dimensional (2D) crystals in the bilayer of liposomes as a means to achieve high-resolution, and subsequent buffer modification as a method to capture snapshots of membrane proteins in action.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Services Biozentrum > BioEM Lab (Chami)
UniBasel Contributors:Chami, Mohamed
Item Type:Article, refereed
Article Subtype:Further Journal Contribution
Publisher:Walter de Gruyter GmbH
Note:Publication type according to Uni Basel Research Database: Journal item
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Last Modified:01 Oct 2020 10:43
Deposited On:01 Oct 2020 10:43

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