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Here, we report a novel computational method that uses an effective scoring function to quantify the binding strength of HA-receptor interactions with high accuracy and speed.
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However, cell-binding assays require specific considerations to accurately quantify the binding affinity of a protein protein interaction.
Ligand binding assays quantify the binding affinities such as Kd or IC50 values.
The fraction of beads that detached at a given force was used to quantify the bead binding strength to the cell.
A final screen was performed to quantify the likely binding strength of each HSE subunit from its sequence similarity with the canonical motif, and to define boundaries of HSEs.
Also, to date, most studies have focused on a population of cells and few groups have quantified the accurate binding strength between specific molecules and single infected cells.
The binding strength is determined by the binding free energy, Δ G bind.
The binding strength and the number of binding sites were determined at different ionic strengths.
The binding strength was significantly weakened by carboxymethylation.
"For an effective drug, you would want to increase the binding strength significantly.
We analyzed in detail the binding strength for maximal flow.
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