Disease relevance of Protein Renaturation

• We report herewith that the Escherichia coli EF-Tu interacts with unfolded and denatured proteins as do molecular chaperones that are involved in protein folding and protein renaturation after stress [1].

High impact information on Protein Renaturation

• Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein [2].
• One might expect that such an activity of DnaJ would promote denatured protein renaturation versus proteolysis [3].
• We report here that Escherichia coli thioredoxin and thioredoxin reductase interact with unfolded and denatured proteins, in a manner similar to that of molecular chaperones that are involved in protein folding and protein renaturation after stress [4].
• Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation [5].
• L-Arginine (L-Arg) has been widely used as an enhancer of protein renaturation [6].

Anatomical context of Protein Renaturation

• However, when the nitrocellulose membranes were treated with a Triton-based buffer to assist in protein renaturation, MAbs 2A5 and 6G7 recognized the two major capsid proteins with molecular masses of 80 and 170 kDa [7].

Associations of Protein Renaturation with chemical compounds

• Protein renaturation by the liquid organic salt ethylammonium nitrate [8].
• It has been recognized that the artificial chaperone system, cetyltrimethylammonium bromide and beta-cyclodextrin, is effective for enhancing protein renaturation [9].
• Stabilization of I" against irreversible aggregation by glycerol results in increased yield of the protein refolding and a complex temperature dependence of the protein renaturation [10].

Gene context of Protein Renaturation

• PNIPAAm exhibited similar behavior as PEG on the renaturation of beta-lactamase in terms of temperature effect and concentration effect, indicating that the mechanism for enhanced protein renaturation for the two polymers might be similar [11].

References