Biological insights from SMA-extracted proteins
Autor: | Philip Kitchen, Roslyn M. Bill, Alejandro Ronco-Campaña, Lucas Unger, Alice Rothnie |
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Rok vydání: | 2021 |
Předmět: |
Maleic acid
Cryo-electron microscopy Protein Conformation Kinetics Lipid Bilayers Biophysics cryo-electron microscopy 02 engineering and technology Biochemistry Divalent 03 medical and health sciences chemistry.chemical_compound Electron transfer Membrane Lipids Biochemical Techniques & Resources Structural Biology Lipid bilayer Review Articles 030304 developmental biology chemistry.chemical_classification 0303 health sciences SMALP protein complexes Molecular Interactions Protein Stability Cryoelectron Microscopy Maleates Membrane Proteins 021001 nanoscience & nanotechnology SMA protein–lipid interactions chemistry Membrane protein Polystyrenes Cell Membranes Excitation & Transport 0210 nano-technology Protein Binding |
Zdroj: | Biochemical Society Transactions |
ISSN: | 1470-8752 |
Popis: | In the twelve years since styrene maleic acid (SMA) was first used to extract and purify a membrane protein within a native lipid bilayer, this technological breakthrough has provided insight into the structural and functional details of protein–lipid interactions. Most recently, advances in cryo-EM have demonstrated that SMA-extracted membrane proteins are a rich-source of structural data. For example, it has been possible to resolve the details of annular lipids and protein–protein interactions within complexes, the nature of lipids within central cavities and binding pockets, regions involved in stabilising multimers, details of terminal residues that would otherwise remain unresolved and the identification of physiologically relevant states. Functionally, SMA extraction has allowed the analysis of membrane proteins that are unstable in detergents, the characterization of an ultrafast component in the kinetics of electron transfer that was not possible in detergent-solubilised samples and quantitative, real-time measurement of binding assays with low concentrations of purified protein. While the use of SMA comes with limitations such as its sensitivity to low pH and divalent cations, its major advantage is maintenance of a protein's lipid bilayer. This has enabled researchers to view and assay proteins in an environment close to their native ones, leading to new structural and mechanistic insights. |
Databáze: | OpenAIRE |
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