Abstract
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 language | English (US) |
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Pages (from-to) | 201-203 |
Number of pages | 3 |
Journal | FEBS Letters |
Volume | 286 |
Issue number | 1-2 |
DOIs | |
State | Published - Jul 29 1991 |
Keywords
- Chaperonin 10
- Chemical synthesis
- GroES
- Heat-shock protein
- Protein folding
- Rubisco
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology