Insight into the Conformation of Protein Folding Intermediate(s) Trapped by GroEL
Open Access
- 1 February 1998
- journal article
- Published by Elsevier
- Vol. 273 (7) , 3915-3925
- https://doi.org/10.1074/jbc.273.7.3915
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein MisfoldsJournal of Molecular Biology, 1995
- Probing the solution structure of the DNA‐binding protein Max by a combination of proteolysis and mass spectrometryProtein Science, 1995
- Destabilization of the complete protein secondary structure on binding to the chaperone GroELNature, 1994
- Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroESFEBS Letters, 1994
- X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferaseJournal of Molecular Biology, 1992
- Different conformations for the same polypeptide bound to chaperones DnaK and GroELNature, 1992
- Binding of a chaperonin to the folding intermediates of lactate dehydrogenaseBiochemistry, 1991
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- Molecular cloning and invivo expression of a precursor to rat mitochondrial aspartate aminotransferaseBiochemical and Biophysical Research Communications, 1987
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970