Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Haloferax volcanii | - |
- |
- |
Renatured (Comment) | Organism |
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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 | Escherichia coli |
study on kinetic folding of urea-denaturedc dihydrofolate reductase and comparison with Escherichia coli 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 | Haloferax volcanii |