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Exact(8)
The binding pocket is formed by 5 helices (helices h4 h8) of the C-terminal domain (Fig. 1b, 3a).
The binding pocket is formed by three tryptophans (Trp-prism) coordinating the quaternary ammonium group of glycine betaine in the closed-liganded structure.
Its binding pocket is formed by nine residues that have at least one heavy atom with a distance within 5 Å [55] to Imipenem, as labeled in Fig. 3B.
The remainder of the binding pocket is formed by Thr80 and Tyr77 and the 5′-FDA molecule.
The predicted binding pocket is formed by the large α-helix and loop of HA2 and a loop consisting of amino acids 300 310 of HA1.
The emetine binding pocket is formed at the interface between 18S rRNA helices 23, 24, 45, and the C-terminus of uS11.
Similar(52)
The trimethylated lysine binding pocket was formed by the following five aromatic residues: H37, Y42, Y62, W65, and W69 (Fig. 2B and 2C).
In the presence of the α-helix, a narrow pantothenic acid-binding pocket is formed making it impossible for statins to bind.
The variability in these four ADP-binding sites may relate to the fact that the ADP-binding pocket is formed by 12 amino acids and that not all of these are critical.
The hydrophobic ligand-binding pocket is formed by the Bet v 1-like core.
As we examined structures of proteins with inhibitor bound in the active site, we have compared active and inactive proteins in which the substrate-binding pocket is formed.
More suggestions(16)
binding pocket is flanked
binding geometry is formed
binding pocket is computed
binding kinetochore is formed
binding interface is formed
binding pocket is summarized
binding pocket is displayed
binding pocket is expected
binding domain is formed
binding unit is formed
binding groove is formed
binding pocket is located
binding pocket is assumed
binding pocket is indicated
binding pocket is seen
binding pocket is lined
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