INTERMOLECULAR FORCES AND ENERGIES BETWEEN LIGANDS AND RECEPTORS

The recognition mechanisms and dissociation pathways of the avidin-bio tin complex and of actin monomers in actin filaments were investigated . The unbinding forces of discrete complexes of avidin or streptavidin with biotin analogs are proportional to the enthalpy change of the co mplex formation but independent of changes in the free energy. This re sult indicates that the unbinding process is adiabatic and that entrop ic changes occur after unbinding. On the basis of the measured forces and binding energies, an effective rupture length of 9.5 +/- 1 angstro ms was calculated for all biotin-avidin pairs and approximately 1 to 3 angstroms for the actin monomer-monomer interaction. A model for the correlation among binding forces, intermolecular potential, and molecu lar function is proposed.