EC Number   |
General Stability |
Reference |
|---|
    1.5.1.3 | 2-mercaptoethanol, 4 mM, stabilizes purified preparation, inclusion in purification steps causes loss of activity |
392232 |
| 1.5.1.3 | 4°C, without urea, 50% loss of activity |
392272 |
| 1.5.1.3 | 50% residual activity in 4 M urea |
673502 |
| 1.5.1.3 | 7,8-dihydrofolate and folate protect against ethoxyformic anhydride modification |
392240 |
| 1.5.1.3 | 7,8-dihydrofolate protects against heat inactivation |
392240, 392245 |
| 1.5.1.3 | 7,8-dihydrofolate protects against inactivation |
392240, 392267 |
| 1.5.1.3 | addition of NaCl (0500 mM concentration) induces significant structural formation to the enzyme. Protein stability increases depending on NaCl concentration regardless of structural formation, and HjDHFR P1 achieves the same stability as the Escherichia coli enzyme at 750 mM NaCl |
729698 |
| 1.5.1.3 | are more mobile. Betweeen EcDHFR and TmDHFR there is a shift in melting temperature of 26 K |
765539 |
| 1.5.1.3 | at ionic strengths below the intracellular ion concentration-derived ionic strength in Escherichia coli ( at or below 0.237 M), the DHFR M20 loop tends to adopt open/closed conformations, and rarely an occluded loop state. As the ionic strength exceeds the physiological ionic strength of 0.237 M, the loop tends to adopt a closed/occluded conformation. the solution ionic strength affects the M20 loop stability differently depending on its conformation: High ionic strengths stabilize the occluded conformation more than low ionic strengths, as Ca2+ ions can approach E17 of the M20 loop and stabilize its orientation, whereas they are distal from the E17 at low ionic strengths. Both low and high ionic strengths can stabilize the closed conformation, |
765136 |
| 1.5.1.3 | bovine serum albumin protects against inactivation |
392258 |
