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To demonstrate that the matched protein was specific for Mycobacterium, we performed another blast analysis in which the organism was limited in all species.
The search for matched protein was later done by using peptide mass fingerprinting (PMF) method in which peptides' masses attained from MALDI were incorporated as the fingerprint in Mascot database.
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This indicates that although there are significant matches, but it is hard to determine the preferred one since these matched proteins are highly similar in predicted secondary structure.
All of the protein spots were successfully identified with confidence interval % (CI %) values >95%% and the matched proteins were obtained from the IPI database.
When the pI and MW of matched proteins were not available, these values were calculated using ExPASy Compute pI/Mw tool.
Using the above-mentioned proteins of D. melanogaster as search queries, we found that L. striatellus encodes homologs of JAK, Domeless, and STAT (Table 3), suggesting it contains a JAK/STAT cascade and that these matched proteins are conserved during insect evolution.
Each matched protein spot was assigned a unique sample spot protein number.
Although our study demonstrated BP3 could bind and activate γδ T cells, we had not yet determined whether its matched protein could be recognized by γδ T cells.
Figure 6 shows that for all species the proportion of matched proteins that are either nuclear or extracellular is greater than for animals generally [41].
The matched proteins that are truly associated with cell cycle process in msiDBN were around 75, which was much higher than JNMF and AVG method.
The gels were CBB stained, matching protein spots were excised and 30 spots were successfully identified by MALDI-TOF MS. Of the identified spots, 19 represented known lumen proteins while the remainder were stroma proteins or proteins of unknown localisation.
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