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To measure the strength of interaction between the two peptides in the c-Fos c-Jun and c-Fos c-Jun c-Fos c-Junthe andolute free energy of binding was c-Jun c-Junusing the MM/GBSA method.

The chemical shift of the PHD1KDM5B backbone atoms amide 1H and 15N after H3K4me0 peptide binding was calculated using the following equation: Δ δ av = 0.5 × Δ δ ( NH) 2 + 0.2 × Δ δ 15 N 2 1 / 2. (B) Ribbon representation of free PHD1KDM5B.

The percentage of binding was calculated using the formulation: % = 100* OD450 of labeled scFvFc + unlabeled scFvFc)/(OD450 of labeled scFvFc + PBS).

The cumulative binding was calculated using equation (2) as described previously.

The percentage in vitro binding or nonspecific binding was calculated using the following equation: percentage binding=(γ after incubation/ γ before incubation) × 100.

The total surface area available for IO- MHPC binding was calculated using the average size of PCPP nanospheres and found to be 123.2 cm/mg polymer.

Free energy of binding was calculated using a previously reported model, where the substrate analogue 5′-CCA-Ala was docked into the isolated INS domain (residues 242 388) of Ef ProRS.

The number of binding sites and binding constants were calculated using a double logarithm regression equation.

The partial charges for the ligand binding site were calculated using the MMFF94x force field and the ligand partial charges were calculated with AM1BCC charges [51, 52].

The binding constants were calculated using Origin provided by ITC200.

The kinetic binding parameters were calculated using the software of the manufacturer.