ArticleEuropean biophysics journal : EBJ2008
Optical tweezers to study single protein A/immunoglobulin G interactions at varying conditions.
Article in European biophysics journal : EBJ, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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.
The trial behind it
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
5 citing papers in PubMed.
- Single-molecule force measurement via optical tweezers reveals different kinetic features of two BRaf mutants responsible for cardio-facial-cutaneous (CFC) syndrome.Biomedical optics express · 2013Article
- Optical tweezers studies on Notch: single-molecule interaction strength is independent of ligand endocytosis.Developmental cell · 2012Article
- Adhesion through single peptide aptamers.The journal of physical chemistry. A · 2011Article
- DNA condensation by TmHU studied by optical tweezers, AFM and molecular dynamics simulations.Journal of biological physics · 2011Article
- Binding and cleavage of E. coli HUbeta by the E. coli Lon protease.Biophysical journal · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Optical tweezers (OT) are ideally suited to study the interaction of single receptor-ligand bonds. Here we introduce a newly developed assay using OT to investigate the interactions between Protein A from Staphylococcus aureus and Immunoglobulin G from rabbit serum (RIgG). We demonstrate that the rupture forces depend on the loading rate and on the sodium chloride concentration. The measured loading rate effect is well known in the literature and the data we obtained were found to be in good agreement with an already published theoretical model. The dependence of the rupture forces on the salt concentration demonstrates the influence of hydrophobic interactions on the bond strength. Our experimental setup can probe the interaction between a single receptor and its specific ligand under changing conditions and hence offers manifold applications in single molecule biotechnology.
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18379774What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.