| Title |
Intermolecular Forces and Energies Between Ligands and Receptors
|
|---|---|
| Published in |
Science, October 1994
|
| DOI | 10.1126/science.7939660 |
| Pubmed ID | |
| Authors | |
| 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 interaction. A model for the correlation among binding forces, intermolecular potential, and molecular function is proposed. |
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Mendeley demographics
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United States | 9 | 4% |
| United Kingdom | 4 | 2% |
| Germany | 4 | 2% |
| Netherlands | 2 | <1% |
| Norway | 1 | <1% |
| Japan | 1 | <1% |
| Italy | 1 | <1% |
| France | 1 | <1% |
| Unknown | 218 | 90% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 67 | 28% |
| Researcher | 46 | 19% |
| Professor | 22 | 9% |
| Student > Master | 21 | 9% |
| Student > Bachelor | 14 | 6% |
| Other | 40 | 17% |
| Unknown | 31 | 13% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 45 | 19% |
| Physics and Astronomy | 44 | 18% |
| Chemistry | 40 | 17% |
| Engineering | 29 | 12% |
| Biochemistry, Genetics and Molecular Biology | 20 | 8% |
| Other | 28 | 12% |
| Unknown | 35 | 15% |