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Our results confirm that changes in affinity and stability for mutant complexes are predictive parameters of resistance as validated by experimental and clinical data.
These results establish that RFS-1/RIP-1 K56A and E138A mutant complexes are compromised for inducing or maintaining the filament in a flexible high FRET state, consistent with their defects in filament remodeling and mediator activity in ensemble experiments.
Our kinetic data show that the GEF activity of these mutant complexes are unaffected, indicating that this interaction is not essential for the activation of the Rabex-5 GEF activity.
We hypothesized that formation of the Tim9 Tim10 complex shields the small Tim proteins from degradation and the Tim9 mutants leave Tim10 vulnerable to degradation because the mutant complexes are unstable and/or more dynamic than the WT complex.
The profiles of inhibitor-induced Tm shifts for wild-type CDK9/cyclin T and the mutant complexes are very similar (R > 0.93 for all combinations of CDK9/cyclin T variants tested).
In contrast, at the Dbp EP site, where mutant CLOCKΔ19 BMAL1 complex can be seen binding as both single CB1 and tandem CB2 complexes, the affinities of the two mutant complexes are similar and lower than wild-type CLOCK BMAL1 complex.
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The loss of activity in these two double-cysteine-pair mutant complexes was attributed to the disulfide bond between the head domain of ISP and cytochrome b and not the one between the tail domain of ISP and cytochrome b.
Also, the subunit composition of the two mutant complexes is the same as the wild type complex (Figure 3D).
The results showed that both mutant complexes were sensitive to trypsin digestion.
Some systems of scFv anti-p17 mutant complexes were not stable and RMSD still did not converge after 10 ns.
Docking score and atomic contact energy (ACE) of the native and mutant complexes were calculated using Patch Dock (Table 4).
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