publication . Article . Other literature type . 1994

Intermolecular forces and energies between ligands and receptors

Ernst-Ludwig Florin; Vincent T. Moy; Hermann E. Gaub;
Restricted
  • Published: 14 Oct 1994 Journal: Science, volume 266, pages 257-259 (issn: 0036-8075, eissn: 1095-9203, Copyright policy)
  • Publisher: American Association for the Advancement of Science (AAAS)
Abstract
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...
Subjects
free text keywords: Multidisciplinary, Binding energy, Chemical physics, Avidin, biology.protein, biology, Monomer, chemistry.chemical_compound, chemistry, Dissociation (psychology), medicine.symptom, medicine, Ligand, Streptavidin, Intermolecular force, Stereochemistry, Enthalpy
Any information missing or wrong?Report an Issue