Abstract
Membrane proteins evolved to reside in the hydrophobic lipid bilayers of cellular membranes. Therefore, membrane proteins bridge the different aqueous compartments separated by the membrane, and furthermore, dynamically interact with their surrounding lipid environment. The latter not only stabilizes membrane proteins, but directly impacts their folding, structure and function. In order to be characterized with biophysical and structural biological methods, membrane proteins are typically extracted and subsequently purified from their native lipid environment. This approach requires that lipid membranes are replaced by suitable surrogates, which ideally closely mimic the native bilayer, in order to maintain the membrane proteins structural and functional integrity. In this review, we survey the currently available membrane mimetic environments ranging from detergent micelles to bicelles, nanodiscs, lipidic-cubic phase (LCP), liposomes, and polymersomes. We discuss their respective advantages and disadvantages as well as their suitability for downstream biophysical and structural characterization. Finally, we take a look at ongoing methodological developments, which aim for direct in-situ characterization of membrane proteins within native membranes instead of relying on membrane mimetics.
Highlights
The overwhelming majority of scientific articles on membrane proteins introduces this class of proteins by mentioning their contribution of roughly 30% to organisms’ genomes, highlighting their importance and resulting self-explanatory relevance
We take a look at ongoing methodological developments, which aim for direct in-situ characterization of membrane proteins within native membranes instead of relying on membrane mimetics
Multiple membrane proteins could be characterized in several different mimetics, allowing the direct comparison and revealing the influence of the different mimetics on the structure and dynamics of these membrane proteins
Summary
The overwhelming majority of scientific articles on membrane proteins introduces this class of proteins by mentioning their contribution of roughly 30% to organisms’ genomes, highlighting their importance and resulting self-explanatory relevance. Similar alterations of behavior and infant mortality in captivity have been reported for several different species, whereupon the degree of these alterations is directly correlated to the extent of the environmental difference, but rarely as pronounced as in polar bears [3] Much like this admittedly farfetched example, membrane proteins evolved to reside in the very specific amphipathic lipid bilayer environment of biological membranes and their removal from this environment often results in pronounced structural and functional ramifications [4,5,6]. Cellular membranes formed a large variety of chemically very [8], ranging from hundreds of different lipid species in “simple”. We survey brane mimeticavailable systems,membrane weigh theirmimetic advantages, as well as their the currently systems, weigh theirdisadvantages, advantages, asevaluate well as how they impact the structural and functional states of membrane proteins and assess their suitability for various biophysical methods
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