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Proteins can be affected either by introducing covalent bindings, interfering through weak, but multiple non-covalent interactions, or the deposition of lipophilic compounds in hydrophobic regions of proteins e.g. within substrate binding pockets, which may cause loss of activity, total inhibition, or degradation.
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The authors report variations in the adamantane-binding pocket which may explain the broad range of responses to inhibitors reported for diverse HCV genotypes (OuYang et al., 2013).
The side-chain of Cys-269 sits at the bottom of the D-alanine-binding pocket which may make VDW clash with the methyl side-chain of L-Alanine.
In comparison with the S5 S1 pockets, the prime-side binding pockets, which interact with the P′ residues downstream of the cleavage junction, are less well defined.
Three α-helices (α2, α3, and α4) lying over the antiparallel β-sheet and loop linking α2 with α3 form a wide pocket, which may play a role of hydrophobic binding pocket.
This observation may be related to the fact that F764 makes direct ligand contact [37], and its replacement by ligand may alter the conformation of the ligand binding pocket which results in increased affinity for ligands other than DHT.
One approach is to identify molecules that occupy the pterin binding pocket which is distinct from the pABA binding pocket that binds sulfonamides.
FhGAPDH lacks a binding pocket which has been exploited in the design of novel antitrypanosomal compounds.
Additionally, the SRL is proposed to host several cation-binding pockets, which could facilitate platinum coordination.
The anchor residues for HLA-A2 fit into narrow and specific-binding pockets, which allow almost only P2 Met and Leu for pocket B and Pc Val and Leu for pocket F (Guo et al., 1993).
FKBP52, in addition to the classic C-terminal MEEVD motif, recognises amino acids at the ATP binding pocket [85], which may impinge on p23 interaction.
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