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The multiple alignment shown in Fig. S2 for the β-barrel domains was used to derive average hydropathy, amphipathicity and similarity plots (Fig. 5).
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Multiple alignment showed that the deduced LhSorP5CS amino acid sequence exhibited high homology with other P5CS proteins from plants, such as MaAAAP5CS (83%), TaP5CS (77%), OsP5CS1 (79%), and ZmP5CS (79%).
The multiple alignment showed high sequence similarity to other thrombin-like enzymes from snake venoms.
In each position of the family, multiple alignment shows an average identity of amino acids of ∼30%.
Multiple alignment showed higher identity and similarity between the C termini of paralogs, which contain the functional portion of the proteins.
Examination of sequences in the multiple alignment shows not only that Cys tends to occur every third residue in the carboxyl-terminal region, but also that differences between closely related sequences commonly feature tripeptide indels.
Multiple alignment showed that the highly conserved DBD is located close to the N-terminal in all the cotton Hsf proteins (Table 2, Figure 1), and comprises 83, 94, 102 or 105 amino acid residues.
Multiple alignment showed a premature stop codon, which prevents the encoding of the conserved cysteine residue at the E2 active site, and an intron that is spliced in E2 homologues, but not in GhGDRP85.
DNA sequence homology analysis with multiple alignment showed that the nucleotide sequences of mutY-amplicons from symbionts in clade II except for Rma showed greater similarity to that of the C. phaseoliformis symbiont (greater than 90%), while the identity with Rma was lower 80-900%).
In addition, a multiple alignment showed that intron 2 from Calliphorinae species, such as T. calliphoroides, A. grahami, C. vicina, and C. lata, differed from those of the Luciliinae species, such as H. ligurriens, L. caesar, L. illustris, L. ampullaceal, and L. sericata (Table 2).
Multiple alignment showed that TaLCYB shared a significant degree of sequence identify with other LCYB proteins in monocots (86.3% sequence identity with OsLCYB from O. sativa, 86.2% with ZmLCYB from Z. mays), and relatively lower homology with LCYB proteins from dicot species, such as C. annuum, A. thaliana, S. lycopersicum (67.4%, 67.1% and 66.5% respectively).
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