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Exact(4)
We hypothesized that the modified form of MEKK1 that we see in our assays (Figure 3B, MEKK1 upper bands) may be due to phosphorylation of multiple sites in MEKK1.
These bands may be due to occurrence of splice variants or post-transational modification, i.e phosphorylation.
Smaller bands may be due to partial proteolysis of the C-terminal regulatory domain, whereas larger bands may be due to alterred migration resulting from bound lipid or detergent molecules.
The remaining 10 with no bands may be due to failed PCR, bad primers, or poor assemblies because all of them have higher expression counts.
Similar(56)
The broadness of the band may be due to existence of these groups in opposite sides.
Therefore, this band may be due to the Si O stretching band of newly formed relatively ordered structure.
The latter band may be due to PO-H bending vibration indicating that the complex formed is protonated.
The other low intensity band may be due to processing intermediates and degradation products.
This slower mobility-shifted band may be due to hyperphosphorylated HSF1 which correlated with hyperactivated HSF1 following heat shock and proteasomal stress (15).
Figure 1 b-c), shows a difference in the positions and area of ν1 b-c ν2 abshowsions bandifferenceay be due to the changed condinions of formathen of sampositionsurfandareaassisted profess.
The results showed that there are similarities and differences in the RNA bands, which may be due to the large amount of tissue sampled with conventional biopsy and the relatively small number of cells sampled with the microbiopsy.
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