Chemical synthesis of 10 kDa chaperonin Biological activity suggests chaperonins do not require other molecular chaperones

Paolo Mascagni, Mirta Tonolo, Haydn Ball, Marguerita Lim, R. John Ellis, Anthony Coates

Research output: Contribution to journalArticle

16 Scopus citations


Molecular chaperones are required for the correct folding and assembly of certain other polypeptides. It is not known whether molecular chaperones themselves require other chaperones to become functional. A 97-amino acid chaperone, the chaperonin 10 protein was chemically synthesised so that during synthesis and purification there was no contact of the chaperone with any other protein. The purified, synthetic chaperonin 10 protein formed oligomeric structures spontaneously and was biologically active as a chaperonin. This is the first description of a chemically synthesised chaperonin, and suggests that no other chaperones are required for correct folding, polymerisation and biological activity of this chaperone.

Original languageEnglish (US)
Pages (from-to)201-203
Number of pages3
JournalFEBS Letters
Issue number1-2
Publication statusPublished - Jul 29 1991



  • Chaperonin 10
  • Chemical synthesis
  • GroES
  • Heat-shock protein
  • Protein folding
  • Rubisco

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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