ArticleBiophysical journal2010
Force-induced lysozyme--HyHEL5 antibody dissociation and its analysis by means of a cooperative binding model.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 9 citations in OpenAlex.
- Mechanical control of antigen detection and discrimination by T and B cell receptors.Biophysical journal · 2024Review
- Digital holography-based 3D particle localization for single-molecule tweezer techniques.Biophysical journal · 2022Article
- Energy Landscape of Alginate-Epimerase Interactions Assessed by Optical Tweezers and Atomic Force Microscopy.PloS one · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dynamic force spectroscopy probes the kinetic properties of molecules interacting with each other such as antibody-antigen, receptor-ligand, etc. In this article, a statistical model for the dissociation of such cooperative systems is presented. The partner molecules are assumed to be linked by a number of relatively weak bonds that can be grouped together into cooperative units. Single bonds are assumed to open and close statistically. Our model was used to analyze molecular recognition experiments of single receptor-ligand pairs in which the two molecules are brought into contact using an atomic force microscope, which leads to the formation of a strong and specific bond. Then a prescribed time-dependent force is applied to the complex and the statistical distribution of forces needed to pull the molecules completely apart is measured. This quantity is also calculated from our model. Furthermore, its dependence on the model parameters, such as binding free energy, number of bonds and groups, number of cooperative elementary bonds and degree of cooperativity within a group, influence of the force on the binding free energy, and the rate of change of the pulling force, is determined.
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Registered trials
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