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Recent advances in membrane mimetics for membrane protein research
Membrane proteins are a highly relevant class of biological molecules and comprise ∼60% of current drug targets. Before being analyzed by structural, biochemical, and biophysical methods, membrane proteins must first be extracted from cellular membranes — often using detergents. Detergent-extracted...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Portland Press Ltd.
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10317169/ https://www.ncbi.nlm.nih.gov/pubmed/37345653 http://dx.doi.org/10.1042/BST20230164 |
Sumario: | Membrane proteins are a highly relevant class of biological molecules and comprise ∼60% of current drug targets. Before being analyzed by structural, biochemical, and biophysical methods, membrane proteins must first be extracted from cellular membranes — often using detergents. Detergent-extracted membrane proteins are amenable to analysis by structural, biochemical, and biophysical techniques. In certain cases, however, detergents can disturb native protein conformations and/or biological activity. This has led to the development of membrane mimetics, which stabilize membrane proteins in a native membrane-like environment that is water-soluble and detergent-free. This review provides an overview of recent developments in the membrane mimetic field, with a focus on nanodiscs, Saposin lipid nanoparticles (SapNPs), peptidiscs, and SMA lipid particles (SMALPs) — and highlights their utility for supporting biophysical, biochemical, and structural characterization of membrane proteins and complexes. |
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