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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.
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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.
Dock score which is actually the strength of the non-covalent interactions among multiple molecules within the binding pocket of a target protein.
The binding pocket of a protein is characterized using the distance dependent, knowledge-based pair potentials of the DrugScore scoring function [2] in combination with multiple ligand atom probes.
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.
Structure-based approaches, like DOCK [3, 4] or PLANTS [5], try to dock the ligand into the binding pocket of a target protein, which requires X-ray diffraction or nuclear magnetic resonance spectroscopy experiments to obtain three-dimensional coordinates of the protein structure.
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.
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