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, 9-12
- 29 March 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 320 (1) , 83-84
- https://doi.org/10.1016/0014-5793(93)81663-k
Abstract
No abstract availableKeywords
This publication has 4 references indexed in Scilit:
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- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperaturesJournal of Bacteriology, 1989
- Homologous plant and bacterial proteins chaperone oligomeric protein assemblyNature, 1988