Báo cáo Y học: Refolding of the Escherichia coli expressed extracellular domain of a7 nicotinic acetylcholine receptor Cys116 mutation diminishes aggregation and stabilizes the b structure
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Heterologous expression of the extracellular domains (ECDs) of the nicotinic acetylcholine receptor (AChR) subunits may give large amounts of proteins for studying the functional and spatial characteristics of their ligand-binding sites. The ECD of the a7 subunit of the homo-oligomeric a7 neuronal AChR appears to be a more suitable object than the ECDs of other heteromeric neuronal or muscle-type AChRs. The rat a7 ECDs (amino-acid residues 1–210) were recently expressed in Escherichia coli as fusion proteins with maltose-binding protein...
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Báo cáo Y học: Refolding of the Escherichia coli expressed extracellular domain of a7 nicotinic acetylcholine receptor Cys116 mutation diminishes aggregation and stabilizes the b structure
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Báo cáo Y học: Refolding of the Escherichia coli expressed extracellular domain of a7 nicotinic acetylcholine receptor Cys116 mutation diminishes aggregation and stabilizes the b structure
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