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However, extensive interactions are also established between the single-strand portion of DNA and the protein binding pocket of a crystallographically related β-clamp molecule.
Site-directed mutagenesis revealed that an arginine side-chain located in the deep binding pocket of a monoclonal antibody (4D5) is essential for binding the neutral polynuclear aromatic hydrocarbon benzo[a]pyrene.
This work provides clues toward uncovering how specificity is achieved within the binding pocket of a polyspecific transporter that may open new possibilities as to how these transporters can be manipulated to bind a designed set of drugs.
In this study, a genetically encoded whole-cell biosensor specifically responding to shikimic acid has been developed by screening a site-saturation mutagenesis library of the binding pocket of a uric acid-responsive regulatory protein.
In a first in silico test, we show that by simultaneously optimizing the sequence and structure of three to nine residue peptide extensions starting from short (1 6 residue) peptide stubs in the binding pocket of a peptide binding protein, the approach can recover both the conformations and the sequences of known binding peptides.
Importantly, our data suggest that while R25/W44 residues located within the binding pocket of a triple-stranded β-fold of WW1 domain are critical for the recognition of PPXY ligands, they are replaced by the chemically distinct E66/Y85 duo at structurally equivalent positions within the WW2 domain, thereby accounting for its failure to bind PPXY ligands.
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The compounds strongly bound to the hydrophobic binding pocket of a-FABP, while showed significantly lower binding affinities to the closely related homologue protein h-FABP.
The molecular basis of spectral sensitivity depends on interactions between amino acids within the binding pocket of an opsin protein and its associated light-sensitive chromophore.
Absorption of a photon of light by the chromophore located in the retinal binding pocket of an opsin causes its photoisomerisation from the 11- cis to an all- trans conformation.
In principle, the substrate binding pocket of an enzyme has to have certain amount of plasticity and even if the stereochemistry of a couple of residues is conserved, possible structural changes due to the plasticity associated with other residues can not be ruled out.
Positive selection at the codon near the binding pocket of the A domain might have an impact on the genetic diversity of mcyC [ 11].
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