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By contrast, at 400 K, all three mutants retained approximately 40% of their α-helical structures during 1.4-μs simulation (Figure S1C, Table 1).
As summarized in Table 2, Q189E and Q189N mutants retained approximately 80 % and 56, respectively, of the catalytic activity of the wild-type COX II, whereas Q189R retained approximately 30% of the catalytic activity.
While the WT exhibited a 53% reduction after 4 min onset of HL, the mutants retained approximately 70% of their photosynthetic activity even after 8 min of HL treatment.
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This mutant retained approximately 65% activity when incubated at 70 °C for 12 h.
A DR0423 knockout mutant, however, retained approximately half of the wild-type level of IR resistance [92], [98].
We were able to demonstrate that the E120Q mutant of NCS-1 [32] retained approximately wild type binding properties with respect to interaction with purified CN.
As reported previously1,11, 5HT-treated wild-type animals retained approximately 40 50% of the body fat seen in vehicle-treated controls, as did the unc-13 mutants (Fig. 1a).
Intestines from dithizone-treated animals retained approximately half the number of Paneth cells compared with controls.
The mutants retained their high resistance to pepsin.
Additionally, these mutants retained the ability to learn much longer than normal worms.
Both mutants retained the global structure of the native protein (Fig. S2e).
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