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There are strong interactions within the chemisorption range for small molecule MOF interactions with defined chemical binding at the metal centers or other specific locations.
These effects have been exploited to develop luminescent systems for the selective recognition of inorganic phosphates, which are discussed on the basis of their structural architecture and mechanism involved in the sensing process triggered by the anion binding at the metal centre(s).
One explanation for this observation may be that the second-largest subunit's contribution to magnesium ion binding at the Metal B site is slightly less critical than the magnesium binding coordinated by the largest subunit.
This infers a combination of effects resulting from anion binding at the metal and interaction with the organic host framework.
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Therefore, we developed in the present study a chronic metal mixture bioavailability model (MMBM) by combining the existing chronic daphnid bioavailability models for Ni, Zn, and Pb with the independent action (IA) model, assuming strict non-interaction between the metals for binding at the metal-specific biotic ligand sites.
The binding of the metal ions at the electrode surface was studied using FTIR.
It has been suggested that these structural differences may arise from the slightly different binding geometries or from a switch from Nɛ to Nδ binding of protein ligands at the metal center in the two ARD isoforms, which may transmit the above described perturbations.
Compared to powder-based metal printing, the process produces "a stronger binding of the metal with virtually the same metallurgy as traditionally-made metal parts".
Lead strongly inhibits ALAD enzyme stoichiometrically and at the molecular level displaces a zinc ion at the metal binding site producing inhibition through a change in the enzyme's quaternary structure.
Based on our experimental findings and pertinent information available on the relevant topic, a mechanism for metal binding at the modified electrode surface is proposed.
The residues involved in metal binding at the di-iron site are widely conserved across the ferritin family with structurally equivalent placements as evident from figures 3, 6A and 7. Subtle differences such as conformational or residue replacement is apparent within the classical ferritins.
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