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. 2019 Mar 27;47(9):4652–4662. doi: 10.1093/nar/gkz188

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© The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 8. — Chaperone activity of IF2 and HSP70 proteins. Refolding of heat-denatured GFP upon incubation for 8 min at 25°C at chaperone/GFP stoichiometric ratios of 1:1 carried out in Buffer containing 1 mM GTP and 1 mM ATP. GFP refolding without chaperone (a) and in the presence of IF2α (b); DnaK, DnaJ and GrpE (c); DnaK, DnaJ, GrpE and IF2α (d) in which the grey part of the bar represents the refolding due to the HSP70 chaperone proteins and the black part represents the increased level of refolding due to the presence of IF2α.