Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL
- 1 April 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 277 (3) , 733-745
- https://doi.org/10.1006/jmbi.1998.1630
Abstract
No abstract availableKeywords
This publication has 66 references indexed in Scilit:
- GroEL-mediated folding of structurally homologous dihydrofolate reductases 1 1Edited by P. E. WrightJournal of Molecular Biology, 1997
- Detection of changes in pairwise interactions during allosteric transitions: Coupling between local and global conformational changes in GroELProceedings of the National Academy of Sciences, 1997
- Release of both native and non-native proteins from a cis-only GroEL ternary complexNature, 1996
- Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.Proceedings of the National Academy of Sciences, 1996
- Determination of Regions in the Dihydrofolate Reductase Structure That Interact with the Molecular Chaperonin GroELBiochemistry, 1996
- Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolutionNature Structural & Molecular Biology, 1995
- The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding.Proceedings of the National Academy of Sciences, 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
- Binding of a chaperonin to the folding intermediates of lactate dehydrogenaseBiochemistry, 1991