Protein Refolding in Nanostructured Reversed Micelles Including a Molecular Chaperone

Research output: Contribution to journalReview article

5 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)275-278
Number of pages4
JournalJournal of Bioscience and Bioengineering
Volume96
Issue number3
DOIs
Publication statusPublished - Jan 1 2003

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Protein Refolding
Molecular Chaperones
Micelles
Proteins
Pancreatic Ribonuclease
Adenosinetriphosphate
Adenosine Triphosphate
Water
Ribonucleases

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Cite this

Protein Refolding in Nanostructured Reversed Micelles Including a Molecular Chaperone. / Sakono, Masafumi; Ichinose, Hirofumi; Goto, Masahiro.

In: Journal of Bioscience and Bioengineering, Vol. 96, No. 3, 01.01.2003, p. 275-278.

Research output: Contribution to journalReview article

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