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Furthermore, the alignment shows that known Myc phosphorylation sites for the human protein (Adhikary and Eilers, 2005), such as glycogen synthase GSK3-targeted Thr58 and MAP-kinase-targeted Ser62, are conserved in both of the medaka Myc proteins.
The amino acid sequence alignment shows that the catalytic antibodies contain a homologous heavy chain sequence in the third complementarity-determining region.
Sequence alignment shows that all SMOs originating from the genus Pseudomonas share the same amino acid residues at positions 73 and 96.
Sequence alignment shows that yArgRS also possesses these three residues on helices H15 and H17 (helices α13 and α15 in eArgRS): E424, K428 and W475 (Fig. 5).
The alignment shows that the amino acids involved in the heme binding as well as those involved in catalysis are highly conserved.
Multiple-sequence alignment shows that these positively charged residues are conserved among many MrkH homologues (Fig. S1), which means that PilZ domain may represent a novel DNA-binding motif.
This alignment shows that the YtvA sequence, (directly) following the conserved DIT motif (amino acids # 125 127, which are key to signal transduction within the YtvA protein (for review: see (van der Steen et al. 2012)) can be fused with a non-cognate kinase domain.
This alignment shows that the C-terminus of β2AR is much longer than that of M2 and D2.
Sequence alignment shows that C285 and C288 are absolutely conserved among the Get3 family members from yeast to human (Fig. 3).
The consistent outcome of various phylogenetic methods based upon this alignment shows that Prod1 arises in a clade comprising only non-mammalian proteins.
A multiple sequence alignment shows that the main part of the sequence is almost identical for all proteins, and differences are observed only in the first 30 35 AAs.
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