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Indirect immunofluorescence assays (IFA) using EBV-infected lymphocytes as the binding substrate are highly sensitive and specific for detecting serum antibodies to viral antigens.
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The site of binding the amino acid substrate is highly conserved in bacterial and eukaryotic GSs, whereas the nucleotide binding site varies to a much larger degree.
The binding between an enzyme and its substrate is highly specific, despite the fact that many different enzymes show significant sequence and structure similarity.
The binding pocket for the phosphothreonine moiety of a phosphorylated FHA substrate is highly conserved in Pellino2.
Recognition of a particular electrophilic substrate is highly dependent upon the residues found within its substrate binding domain (H-site).
Superposition (overlapping of Cα atoms) of modeled AGPase SS with their structural homologue in DS3.5 reveals that the spatial position and orientation of substrate and inhibitor binding site are highly conserved and 4(b) and Figures 5(a) and 5(b)) and shows a very low RMSD within the substrate and inhibitor binding site which is evident from Table 7.
These binding sites are highly charged.
The extreme C-terminal-regulatory EEVD motif of Hsp70, essential for its ATPase activity and substrate binding is highly conserved within the Hsp70 family.
The substrate-binding pocket is highly constrained.
The subunits share 30 to 35% of sequence identity, with the highest level of conservation within the ATPase domain, and the substrate-binding domains being highly divergent [ 114].
However, we noticed that Um02592 contains a high degree of divergence in the substrate-binding and catalytic domains, which are highly conserved between TSRs and HIBDs.
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