The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
Measuring the Forces that Control Protein Interactions
Abstract
Although the force fields and interaction energies that control protein behavior can be inferred indirectly from equilibrium and kinetic measurements, recent developments have made it possible to quantify directly (a) the ranges, magnitudes, and time dependence of the interaction energies and forces between biological materials; (b) the mechanical properties of isolated proteins; and (c) the strength of single receptor-ligand bonds. This review describes recent results obtained by using the atomic force microscope, optical tweezers, the surface force apparatus, and micropipette aspiration to quantify short-range protein-ligand interactions and the long-range, nonspecific forces that together control protein behavior. The examples presented illustrate the power of force measurements to quantify directly the force fields and energies that control protein behavior.
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Cites
Intermolecular and Surface Forces
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Pectins: structure, biosynthesis, and oligogalacturonide-related signaling
Ridley, B. L., O'Neill, M. A., & Mohnen, D. (2001) · Phytochemistry · doi:10.1016/s0031-9422(01)00113-3 · Cited by 1,912
Jalili, N., & Laxminarayana, K. (2004) · Mechatronics · doi:10.1016/j.mechatronics.2004.04.005 · Cited by 610
The power of two: protein dimerization in biology
Marianayagam, N. J., Sunde, M., & Matthews, J. M. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.09.006 · Cited by 599
Accumulation of tau induced in neurites by microglial proinflammatory mediators
Gorlovoy, P., Larionov, S., Pham, T. T. H., & Neumann, H. (2009) · The FASEB Journal · doi:10.1096/fj.08-123877 · Cited by 156
Metadata
- Authors
- Leckband, D.
- Venue
- Annual Review of Biophysics and Biomolecular Structure
- Publisher
- Annual Reviews
- Published
- 2000-06
- Volume
- 29
- Issue
- 1
- Pages
- 1-26
- ISSN
- 1056-8700 (ISSN-L)
- 1545-4266
- OpenAlex
- W2163884154
- Cited by
- 444
- References
- 73
- FWCI
- 6.64
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
