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

Proteoliposomes – a system to study membrane proteins under buffer gradients by cryo-EM Abstract 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nanotechnology Reviews de Gruyter

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

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Publisher
de Gruyter
Copyright
Copyright © 2017 by the
ISSN
2191-9089
eISSN
2191-9097
DOI
10.1515/ntrev-2016-0081
Publisher site
See Article on Publisher Site

Abstract

Abstract 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.

Journal

Nanotechnology Reviewsde Gruyter

Published: Feb 1, 2017

References