Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Issue: 130
Published: Dec 12, 2017
Abstract
Identification of natural ligands of chemoreceptors and structural studies aimed at elucidation of the molecular basis of the ligand specificity can be greatly facilitated by the production of milligram amounts of pure, folded ligand binding domains. Attempts to heterologously express periplasmic ligand binding domains of bacterial chemoreceptors in Escherichia coli (E. coli) often result in their targeting into inclusion bodies. Here, a method...
Paper Details
Title
Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published Date
Dec 12, 2017
Issue
130
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