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Intermolecular Forces and Energies Between Ligands and Receptors
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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Cites
Direct observation of kinesin stepping by optical trapping interferometry
Svoboda, K., Schmidt, C. F., Schnapp, B. J., & Block, S. M. (1993) · Nature · doi:10.1038/365721a0 · Cited by 1,910
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Configurations of fluid membranes and vesicles
Seifert, U. (1997) · Advances in Physics · doi:10.1080/00018739700101488 · Cited by 1,650
Polymer surface modification for the attachment of bioactive compounds
Goddard, J. M., & Hotchkiss, J. H. (2007) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2007.04.002 · Cited by 1,379
Appreciating force and shape—the rise of mechanotransduction in cell biology
Iskratsch, T., Wolfenson, H., & Sheetz, M. P. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3903 · Cited by 798
Dynamic force spectroscopy of single DNA molecules
Strunz, T., Oroszlan, K., Schäfer, R., & Güntherodt, H.-J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11277 · Cited by 580
Izrailev, S., Stepaniants, S., Isralewitz, B., Kosztin, D., Lu, H., Molnar, F., Wriggers, W., & Schulten, K. (1999) · Lecture Notes in Computational Science and Engineering · doi:10.1007/978-3-642-58360-5_2 · Cited by 451
Metadata
- Authors
- Moy, V. T., Florin, E.-L., & Gaub, H. E.
- Venue
- Science
- Published
- 1994-10-14
- Volume
- 266
- Issue
- 5183
- Pages
- 257-259
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2073277085
- Cited by
- 875
- References
- 1
- FWCI
- 15.87
- Type
- journal article
- Language
- en
- Open access
- closed
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- Moy, V. T., Florin, E.-L., & Gaub, H. E. (1994). Intermolecular Forces and Energies Between Ligands and Receptors. Science. https://doi.org/10.1126/science.7939660
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
