Changing the nature of the initial chaperonin capture complex influences the substrate folding efficiency.

Abstract

For the chaperonin substrates, rhodanese, malate dehydrogenase (MDH), and glutamine synthetase (GS), the folding efficiencies, and the lifetimes of folding intermediates were measured with either the nucleotide-free GroEL or the activated ATP.GroEL.GroES chaperonin complex. With both nucleotide-free and activated complex, the folding efficiency of rhodanese… (More)

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Cite this paper

@article{Voziyan1998ChangingTN, title={Changing the nature of the initial chaperonin capture complex influences the substrate folding efficiency.}, author={Paul A. Voziyan and B C Tieman and Chia Mei Low and Mark T. Fisher}, journal={The Journal of biological chemistry}, year={1998}, volume={273 39}, pages={25073-8} }