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Literature summary for 1.5.1.3 extracted from

  • Gloss, L.M.; Topping, T.B.; Binder, A.K.; Lohman, J.R.
    Kinetic folding of Haloferax volcanii and Escherichia coli dihydrofolate reductases: haloadaptation by unfolded state destabilization at high ionic strength (2008), J. Mol. Biol., 376, 1451-1462.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Haloferax volcanii
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Renatured (Commentary)

Renatured (Comment) Organism
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