Calculated K_ds and derived ΔG° (Gibbs free energy of binding) for the interactions between eIF4E and the derivative peptides used to study the relationship of amino acids at positions 8 and 12 in relation to the presence of the V residue present at position 10.

The table shows the peptide sequences used to study the relationship of amino acids at positions 8 and 12 in relation to the presence of the V residue present at position 10. Kds were determined using SPR with eIF4E immobilized via amine coupling on the chip surface. Kds were derived from the equilibrium responses (Keq) and from the association and dissociation phases (Kkin) of the SPR data. The Gibbs free energy of binding (ΔG°) was calculated with the equation ΔG = -RT ln Ka using both dissociation constant values determined.