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Solid-supported lipid bilayers – A versatile tool for the structural and functional characterization of membrane proteins.

Authors :
Andersson, Jakob
Bilotto, Pierluigi
Mears, Laura L.E.
Fossati, Stefan
Ramach, Ulrich
Köper, Ingo
Valtiner, Markus
Knoll, Wolfgang
Source :
Methods. Aug2020, Vol. 180, p56-68. 13p.
Publication Year :
2020

Abstract

• Protein-protein interactions studied with the surface forces apparatus. • Membrane protein structure studied via atomic force microscopy and neutron scattering. • Membrane protein function studied via surface plasmon resonance and electrochemical tools. The cellular membrane is central to the development of single-and multicellular life, as it separates the delicate cellular interior from the hostile environment. It exerts tight control over entry and exit of substances, is responsible for signaling with other cells in multicellular organisms and prevents pathogens from entering the cell. In the case of bacteria and viruses, the cellular membrane also hosts the proteins enabling invasion of the host organism. In a very real sense therefore, the cellular membrane is central to all life. The study of the cell membrane and membrane proteins in particular has therefore attracted significant attention. Due to the enormous variety of tasks performed by the membrane, it is a highly complex and challenging structure to study. Ideally, membrane components would be studied in isolation from this environment, but unlike water soluble proteins, the amphiphilic environment provided by the cellular membrane is key to the structure and function of the cell membrane. Therefore, model membranes have been developed to provide an environment in which a membrane protein can be studied. This review presents a set of tools that enable the comprehensive characterization of membrane proteins: electrochemical tools, surface plasmon resonance, neutron scattering, the surface forces apparatus and atomic force microscopy are discussed, with a particular focus on experimental technique and data evaluation. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
10462023
Volume :
180
Database :
Academic Search Index
Journal :
Methods
Publication Type :
Academic Journal
Accession number :
146483015
Full Text :
https://doi.org/10.1016/j.ymeth.2020.09.005