Domain Motions in GroEL upon Binding of an Oligopeptide
- 28 November 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 334 (3) , 489-499
- https://doi.org/10.1016/j.jmb.2003.09.074
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Mechanism of substrate recognition by the chaperonin GroELBiochemistry and Cell Biology, 2001
- Chaperonin-Mediated Protein FoldingAnnual Review of Biophysics, 2001
- Identification of in vivo substrates of the chaperonin GroELNature, 1999
- STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDINGAnnual Review of Biochemistry, 1998
- A structural model for GroEL–polypeptide recognitionProceedings of the National Academy of Sciences, 1997
- The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγSNature Structural & Molecular Biology, 1996
- Residues in chaperonin GroEL required for polypeptide binding and releaseNature, 1994
- The crystal structure of the bacterial chaperonln GroEL at 2.8 ÅNature, 1994
- Folding in vivo of bacterial cytoplasmic proteins: Role of GroELCell, 1993
- Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteinsProtein Science, 1992