Interaction of GroE with an all-beta-protein.
Open Access
- 1 October 1992
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 267 (24) , 16829-16833
- https://doi.org/10.1016/s0021-9258(18)41858-3
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Different conformations for the same polypeptide bound to chaperones DnaK and GroELNature, 1992
- Binding of chaperoninsNature, 1991
- 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
- Use of fluorescence energy transfer to characterize the compactness of the constant fragment of an immunoglobulin light chain in the early stage of foldingBiochemistry, 1991
- INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINSAnnual Review of Biochemistry, 1990
- Structural Basis of Antibody FunctionAnnual Review of Immunology, 1983
- Unfolding and refolding of the constant fragment of the immunoglobulin light chainJournal of Molecular Biology, 1982
- Purification and properties of groE, a host protein involved in bacteriophage assemblyJournal of Molecular Biology, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976