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Site-directed mutagenesis of the large fragment of DNA polymerase I (Klenow fragment) yielded two mutant proteins lacking 3',5'-exonuclease activity but having normal polymerase activity.
In addition, we investigated the functional capabilities of M2 mutant proteins lacking different combinations of these two putative phosphorylation sites at the biochemical and signalling level.
In Drosophila, the EF-Hand of Nkd alone is required for binding to Dvl [25], but curiously, Nkd mutant proteins lacking the EF-Hand are capable of rescuing nkd-/ mutants to adulthood [26].
The first hints came from overexpression experiments with constitutively active mutant proteins lacking their autoregulatory domains.
By using this approach, we found that M1X and the other mutant proteins lacking the first methionine were detected by the anti-HA antibody.
Despite these observations, the fact that both mutant proteins lacking the CTR (i.e., H1WCT and H4WCT) exhibit an altered sensitivity to ethylene may suggest that HAHB4 CTR could be non-essential for its activity in this pathway.
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As a result, both mutant proteins lack the transmembrane segments.
Because these mutant proteins lack different portions of the N-terminal region, this discrepancy may be explained by the distinct functions of each mutant protein.
As both Wilms2 and Wilms3 mutant proteins lack a functional DNA binding domain, it was of interest to gain more insight into the underlying molecular mechanisms.
In order to start to unravel the redox interactome of T. cruzi we designed an active site mutant protein lacking the resolving cysteine, and validated the complex formation in vitro between the mutated TcTXN1 and a known partner, the cytosolic peroxiredoxin.
While full-length ADNP and the homeodomain alone co-localized with HP1β the mutant protein lacking the homeodomain did not display enrichment at any particular site in the nucleus.
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CEO of Professional Science Editing for Scientists @ prosciediting.com