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Displacement binding data were fitted by nonlinear regression for a one-site binding competition model, unless otherwise noted.
Saturation binding data were fitted by nonlinear regression with a hyperbolic function for a one-binding site model.
The binding data were fitted using the Octet analysis software.
The binding data were fitted to a 1 1 Langmuir interaction model to calculate the rate constants for association (ka) and dissociation (kd) and the equilibrium dissociation constant (KD= kd/ ka) for kinase inhibitor and Nb interactions.
Binding data were fitted to a simple 1 1 binding model.
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First, the binding data were fit to the nonspecific finite lattice DNA binding model (eq 3a).
We therefore analyzed the data using a more sophisticated approach; the R3 (nonspecific) binding data were fit to the nonspecific finite lattice DNA binding model (eq 3a), while the I1 (cos-specific) binding data were simultaneously fit to the competitive specific/nonspecific finite lattice DNA binding model (eq 3b).
Titration binding data were fit according to the equation where Pt is the total S100B protein concentration, Lt is the total IC3 ligand peptide concentration, Kd is the dissociation constant, and N is the maximum chemical shift change upon ligand binding.
Binding data were fit to a Hill equation (eq 1) to account for cooperative binding.
Bead-binding data was fitted with two poisson probability curves using a linear least-squares method (Svoboda and Block, 1994).
Where a level of nonspecific binding >10% of total binding was observed, the dissociation kinetic data were fitted to a 2-phase exponential decay function where Plateau and t are as defined above, and Spanfast and Spanslow represent the proportion of Y0-Plateau accounted for by the fast (koff(fast)) and slow (koff slow)) dissociation rate, respectively.
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