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In a previous study (Ratanapariyanuch et al. 2011), we thoroughly characterized TS to determine the presence of compounds that might affect protein extraction.
This change in peptide sequence might affect protein folding and stability that might alter CRH binding affinity.
Sequencing studies of Eef1a2 transcripts in other tumors would clearly be required to fully exclude the possibility that coding region mutations might affect protein expression.
Also, post-transcriptional and post-translational regulation might affect protein expression.
Thus, apparently inert polymorphisms in a gene might affect protein conformation.
We cannot exclude the possibility that mutating phospho-site amino acids might affect protein function for reasons other than phosphorylation state.
Similar(45)
Methylated TLS is more associated with PRMT1 by in vitro methylation assays, suggesting that arginine-methylation of TLS might affect protein-protein interactions.
(c) Phosphorylated rpS6 might not affect protein synthesis, but instead interacts with cellular protein(s), which consequently becomes active or inactive, and thus affects the cell physiology.
Therefore, we reasoned that OLA1 might instead affect protein stability.
Though protein detection in the transgenic plants is desirable, we did not add an epitope tag to the coding sequence because a tag might negatively affect protein function.
For example, in-frame indels or single base alterations could appear as disruptions by restriction digest, but might not affect protein function.
More suggestions(15)
might impair protein
might affect gene
might affect body
might impact protein
might regulate protein
might affect vaccine
might identify protein
might remove protein
might affect prey
might connect protein
might have protein
might modulate protein
might maintain protein
might control protein
might involve protein
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