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Updated: Aug 1, 2026

Intracellular Refolding Assay
Published on: January 24, 2012
Protein refolding in nanostructured reversed micelles including a molecular chaperone
Masafumi Sakono1, Hirofumi Ichinose, Masahiro Goto
1Department of Applied Chemistry, Graduate School of Engineering, Kyushu University, Hakozaki, Fukuoka 812-8581, Japan.
Abstract:
Reversed micelles including the molecular chaperone GroEL were applied to the protein refolding of denatured RNase A. The molecular chaperone was successfully functionalized in the water pools of the reversed micelles sharing a structural size of 15-25 nm. The refolding yield of RNase A in the reversed-micelle/GroEL system was much greater than that of spontaneous renaturation. The refolding yield mediated by GroEL in the reversed micelles was strongly dependent on the presence of ATP or Mg2+, suggesting that the GroEL hosted in the reversed micelles was biologically active in the micelles. Under the optimum conditions, this novel refolding technique could completely renature the denatured RNase A in 1 h.
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