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Earlier biochemical in vitro studies suggest that each Dscam1 isoform has extracellular domains that prefer to bind to itself (self-binding or homophilic binding), while heterophilic binding (binding between different isoforms) tends to be weak or below the detection limit of the assays used [ 9].
If Fj inhibits Ds binding and promotes Ft binding more strongly to the right, Ft molecules in each cell prefer to bind to Ds in the next left-most cell (with which they have a stronger binding interaction), and so preferentially accumulate at left cell edges; similarly Ds molecules prefer to associate with Ft in the next right-most cell and in turn accumulate at right cell edges.
In the ground state, they prefer to bind bromide ion.
SAR demonstrated that the S2 and S3 pockets of FVIIa prefer to bind small, lipophilic groups.
Solute atoms with larger electronegativity more favorably bond to the vacancy and the smaller ones prefer to bind to the 〈1 1〉-crowdionon, and vice versa.
The tendency of ligands to coordinate with Cu2+ is NH2 > C3OH > H2O > NHCOCH3, suggesting that amine groups (NH2) on chitosan prefer to bind Cu2+ and acetamide groups (NHCOCH3) on chitin lose their coordination with Cu2+ in aqueous solution.
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We postulated that Dxc could be replaced by ACh when the pH of crystallized condition increases since key amino acids around the binding cavity determine ecMdfA prefers to bind positively charged Ach rather than negatively charged Dxc.
The SDS molecule prefers to bind with CD rather than with the metal complex.
While the larger size cation prefers to bind on the concave surface, the smaller cation stabilizes on the convex surface.
Results indicate that the trigger molecule (i.e., sulfate ion) prefers to bind to the rod-like nanoceria (on its unique {1 1 0} facets) rather than nanopolyhedra or nanocubes.
Due to the stronger affinity between Hep and protamine, Hep preferred to bind with it instead of Z-TPE-5 after the addition of protamine, so the fluorescence could be reduced.
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