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Publications in Scientific Journals:

J. Andersson, P. Bilotto, L. Mears, S. Fossati, U. Ramach, I. Köper, M. Valtiner, W. Knoll:
"Solid-supported lipid bilayers - A versatile tool for the structural and functional characterization of membrane proteins";
Methods, 180 (2020), 56 - 68.



English abstract:
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.

Keywords:
Model membranesMembrane proteinsBiophysicsStructural biology


"Official" electronic version of the publication (accessed through its Digital Object Identifier - DOI)
http://dx.doi.org/10.1016/j.ymeth.2020.09.005

Electronic version of the publication:
https://doi.org/10.1016/j.ymeth.2020.09.005


Created from the Publication Database of the Vienna University of Technology.