Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent
- 1 March 1995
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1247 (2) , 209-214
- https://doi.org/10.1016/0167-4838(94)00231-5
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Stabilization of a compact conformation of monomeric GroEL at low temperature by adenine nucleotidesFEBS Letters, 1993
- A comment on: ‘The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60): Evidence for the presence of a single tryptophan’, by N.C. Price, S.M. Kelly, S. Wood and A. auf der Mauer (1991) FEBS Lett. 292, 9-12FEBS Letters, 1993
- The unfolding and attempted refolding of the bacterial chaperone protein groEL (cpn60)Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993
- Promotion of the in vitro renaturation of dodecameric glutamine synthetase from Escherichia coli in the presence of GroEL (chaperonin-60) and ATPBiochemistry, 1992
- Binding of a chaperonin to the folding intermediates of lactate dehydrogenaseBiochemistry, 1991
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- Purification and properties of groE, a host protein involved in bacteriophage assemblyJournal of Molecular Biology, 1979
- Isolation and characterization of the host protein groE involved in bacteriophage lambda assemblyJournal of Molecular Biology, 1979
- The covalent and tertiary structure of bovine liver rhodaneseNature, 1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970