Intermolecular forces and energies between ligands and receptors

Vincent T. Moy, Ernst Ludwig Florin, Hermann E. Gaub

Research output: Contribution to journalArticlepeer-review

785 Scopus citations


The recognition mechanisms and dissociation pathways of the avidin-biotin 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 complex formation but independent of changes in the free energy. This result indicates that the unbinding process is adiabatic and that entropic changes occur after unbinding. On the basis of the measured forces and binding energies, an effective rupture length of 9.5 ± 1 angstroms 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 molecular function is proposed.

Original languageEnglish (US)
Pages (from-to)257-259
Number of pages3
Issue number5183
StatePublished - Jan 1 1994
Externally publishedYes

ASJC Scopus subject areas

  • General


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