Structural and mechanistic consequences of polypeptide binding by GroEL
- 1 December 1997
- journal article
- review article
- Published by Elsevier in Folding and Design
- Vol. 2 (6), R93-R104
- https://doi.org/10.1016/s1359-0278(97)00046-1
Abstract
No abstract availableKeywords
This publication has 87 references indexed in Scilit:
- Binding affinity of proteins to hsp90 correlates with both hydrophobicity and positive charges. A surface plasmon resonance studyLife Sciences, 1997
- Conformational States Bound by the Molecular Chaperones GroEL and SecB: A Hidden Unfolding (Annealing) ActivityJournal of Molecular Biology, 1996
- Allosteric Control by ATP of Non-folded Protein Binding to GroELJournal of Molecular Biology, 1996
- Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein MisfoldsJournal of Molecular Biology, 1995
- The Origins and Consequences of Asymmetry in the Chaperonin Reaction CycleJournal of Molecular Biology, 1995
- Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperoninFEBS Letters, 1995
- VISTAS: A package for VIsualizing STructures and sequences of proteinsJournal of Molecular Graphics, 1995
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- The MIDAS display systemJournal of Molecular Graphics, 1988