Effects of Confinement in Chaperonin Assisted Protein Folding: Rate Enhancement by Decreasing the Roughness of the Folding Energy Landscape
- 2 September 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 332 (3) , 701-713
- https://doi.org/10.1016/s0022-2836(03)00929-x
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Molecular Chaperones in the Cytosol: from Nascent Chain to Folded ProteinScience, 2002
- Molecular chaperones: Inside and outside the Anfinsen cageCurrent Biology, 2001
- Dual Function of Protein Confinement in Chaperonin-Assisted Protein FoldingCell, 2001
- Chaperonin Function: Folding by Forced UnfoldingScience, 1999
- Protein folding Folding with a two-stroke motorNature, 1997
- The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complexNature, 1997
- Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism.Proceedings of the National Academy of Sciences, 1996
- GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative formsCell, 1994
- Dynamics of the Chaperonin ATPase Cycle: Implications for Facilitated Protein FoldingScience, 1994
- Molecular Chaperones: Opening and closing the Anfinsen cageCurrent Biology, 1994