EC Number   |
Reference |
|---|
    1.5.1.3 | both the chaperone systems GroEL (minichaperone) and GroEL-GroES prevent thermal aggregation and assist in refolding of DHFR |
764013 |
| 1.5.1.3 | denaturation with 4 M urea, no renaturation by removing urea by dialysis |
392232 |
| 1.5.1.3 | enzyme denatured with 8 M urea cannot be renatured by removal of urea |
392245 |
| 1.5.1.3 | kinetic of refolding upon dilution of unfolded enzyme in 4.5 M urea to 1.29 M urea |
392214 |
| 1.5.1.3 | NMR measurements of amide proton exchange protection during folding in the presence of methotrextae and ATP either free in solution or inside the stable cavity formed between a single ring variant of GroEL, SR1, and GroES chaperonins. In the SR1-GroES-mediated reaction, recovery of dihydrofolate reductase is twofold higher than in the spontaneous reaction. In both reactions, folding follows the same trajectories |
689773 |
| 1.5.1.3 | refolding after solubilisation from inclusion bodies with 4 M guanidium hydrochloride in 0.5% polyethylene glycol 1450, pH 7.0 |
392281 |
| 1.5.1.3 | refolding of enzyme reversibly unfolded in 7 M urea, effect of several peptide fragments, derived from limited proteolytic cleavage of dihydrofolate reductase on the attainment of the folded state |
392213 |
| 1.5.1.3 | refolding of recombinant enzymes from inclusion bodies due to expression in E. coli |
392287 |
| 1.5.1.3 | sodium docecyl sulfate causes irreversible inactivation |
392215 |
| 1.5.1.3 | study on kinetic folding of urea-denatured dihydrofolate reductase and comparison with Haloferax volcanii enzyme. Folding follows similar kinetics for both enzymes, with a 5-ms stopped-flow burst-phase species that folds to the native state through two sequential intermediateswith relaxation times of 0.1-3 sec and 25-100 sec. The unfolding of Haloferax volcanii enzyme at low ionic strength is relatively slow. Increased KCl concentrations slow the urea-induced unfolding of both enzymes, but much less than expected from equilibrium studies. Unfolding rates are relatively independent of ionic strength |
688397 |
