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From these mechanistic constraints, we conclude these structures of human ASNase cannot represent a mechanistically relevant state and that some structural rearrangement must occur prior to autoproteolysis.
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FATCAT concludes these structures are not similar (P-value of 9.96e-01).
Based on these observations, we can conclude that these structures are products formed from HAuCl4 and 4,4'-bipyridine.
From the Lifeact-mEGFP images it is of course impossible to infer the proteins involved in the event, nor can we conclude that these structures are producing the same forces as seen in the in vitro experiment.
We conclude that these structures conform to the previously described definition of NR structures, specifically type-II NR events (Malhas et al. 2011), and are consistent with DNA, histone and nuclear-GFP signals that are excluded from the interior of these membrane containing structures.
Based on the difference in size, lack of detail in the 1923 description, and the fact this is apparently not the same species of host or symbiont, or the same collection location, it would be premature to conclude these are the same structure.
Their purpose on this site is uncertain however, since at 2 m square they have been considered by archaeologists to be too small for dwellings; as a result, it has been concluded that these structures were probably granaries.
It should be noted that the FtsA-YFP structures at the poles in the min mutant backgrounds persisted and, hence, we concluded that these structures did not reassemble, but instead never completely disassembled.
A molecular docking study was also performed to gain comprehensive understanding into plausible binding modes and to conclude the structure activity relationships of the synthesized compounds.
It can be concluded that, for these structures, buckling is a dominant behavior and the printing direction needs to be considered during the design process.
Moreover, Structure 4 exhibited spatial and spectral characteristics similar to Structure 3. We conclude that Structures 3 and 4 represent the same or very similar neural substrate, differing only in when and how they were activated.
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