Isolation and biochemical characterization of highly purified Escherichia coli molecular chaperone Cpn60 (GroEL) by affinity chromatography and urea-induced monomerization
- 27 September 1995
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1252 (1) , 69-78
- https://doi.org/10.1016/0167-4838(95)00111-7
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- GroEL/ES-mediated refolding of human carbonic anhydrase II: role of N-terminal helices as recognition motifs for GroELBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopyNature, 1994
- The symmetry of Escherichia coli cpn60 (GroEL) determined by X-ray crystallographyJournal of Molecular Biology, 1994
- ChaperoninsCurrent Opinion in Structural Biology, 1993
- Crystallization and preliminary X-ray investigation of theEscherichia colimolecular chaperone cpn60 (GroEL)FEBS 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
- MOLECULAR CHAPERONESAnnual Review of Biochemistry, 1991
- (Mg–ATP)-dependent self-assembly of molecular chaperone GroELNature, 1990
- Homologous plant and bacterial proteins chaperone oligomeric protein assemblyNature, 1988