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Exact(6)
The host harbors the mutant phenylalanyl-tRNA synthetase (PheRS) which has an enlarged binding pocket, where the Ala294Gly/Thr251Gly mutant PheRS (PheRS**) was expressed under the control of T7 promoters.
In other work, scientists have examined a portion of the avian virus known as the receptor binding pocket, where the virus locks on to cells in the infected individual.
X-ray crystal structures of the ligand binding domain of human PXR (hPXR) alone or bound with agonists reveal a highly hydrophobic ligand binding pocket where the aromatic amino acid residue W299 appears to play a critical role in ligand binding.
Of the lysine residues we identified to be acetylated in our study, Lys23 is uniquely positioned at the binding pocket where the electrostatic potential is highest.
The rigid acetylene linkage directs the remaining portion of the drug deep toward the rear corner of the ATP binding pocket where the methylphenyl and 3-trifluoromethylphenyl aromatic rings of the inhibitor engage sites 2 and 3, respectively.
These amino acids are all located at the NS3/4A S2 binding pocket, where the inhibitor's isoquinoline moiety protrudes from the substrate envelope and interacts extensively with the protease.
Similar(54)
The peptide-binding domain is similar to those of E. coli DnaK, and forms a β-sandwich peptide-binding pocket where the peptide-binding cleft is located.
Instead of interacting with the outer crater, the methanesulfonamide group of KL001 is anchored at an outer vestibule of the FAD-binding pocket, where the FBXL3 C-terminal tail enters in the Skp1-FBXL3-CRY2 structure.
This configuration projects the side chain of the amino acid into the binding pocket where it is bound by the remaining 8 amino acids lining the pocket.
The carboxy-terminal flexible tail of the Ubl protrudes into a shallow cleft on the E1 surface and points toward the ATP binding pocket, where it is clamped tightly by the crossover loop connecting the cysteine domain and the active Rossmann-type subunit.
Rats were selected for use because site directed mutagenesis studies indicate that the binding pocket where 5-HT6R antagonists bind in human and rat is similar [13].
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