ArticleProceedings of the National Academy of Sciences of the United States of America2007
A functional single-molecule binding assay via force spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Force writes memory: proline isomerization as a molecular memory switch.Biochemical Society transactions · 2025Review
- Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- A novel design for magnetic tweezers with wide-range temperature control.Biophysical journal · 2023Article
- Tools shaping drug discovery and development.Biophysics reviews · 2022Review
- Mechanical regulation of talin through binding and history-dependent unfolding.Science advances · 2022Article
- Interaction of chloramphenicol with titin I27 probed using single-molecule force spectroscopy.Journal of biological physics · 2021Article
- Modulation of a protein-folding landscape revealed by AFM-based force spectroscopy notwithstanding instrumental limitations.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Effects of Ligand Binding on the Energy Landscape of Acyl-CoA-Binding Protein.Biophysical journal · 2020Article
- Optical imaging of single-protein size, charge, mobility, and binding.Nature communications · 2020Article
- Force-Dependent Binding Constants.Biochemistry · 2019Review
- The Single-Molecule Centroid Localization Algorithm Improves the Accuracy of Fluorescence Binding Assays.Biochemistry · 2018Article
- Force Spectroscopy with 9-μs Resolution and Sub-pN Stability by Tailoring AFM Cantilever Geometry.Biophysical journal · 2017Article
- Rapid Characterization of a Mechanically Labile α-Helical Protein Enabled by Efficient Site-Specific Bioconjugation.Journal of the American Chemical Society · 2017Article
- Single molecule force spectroscopy reveals the effect of BiP chaperone on protein folding.Protein science : a publication of the Protein Society · 2017Article
- Multidomain proteins under force.Nanotechnology · 2017Article
- A HaloTag Anchored Ruler for Week-Long Studies of Protein Dynamics.Journal of the American Chemical Society · 2016Article
- Effects of ligand binding on the mechanical stability of protein GB1 studied by steered molecular dynamics simulation.Journal of molecular modeling · 2016Article
- Modular, Nondegenerate Polyprotein Scaffolds for Atomic Force Spectroscopy.Biomacromolecules · 2016Article
- Cell adhesion manipulation through single cell assembly for characterization of initial cell-to-cell interaction.Biomedical engineering online · 2015Article
- Ligand-induced changes of the apparent transition-state position in mechanical protein unfolding.Biophysical journal · 2015Article
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Authors and funding
4 authors.
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Abstract
Protein-ligand interactions, including protein-protein interactions, are ubiquitously essential in biological processes and also have important applications in biotechnology. A wide range of methodologies have been developed for quantitative analysis of protein-ligand interactions. However, most of them do not report direct functional/structural consequence of ligand binding. Instead they only detect the change of physical properties, such as fluorescence and refractive index, because of the colocalization of protein and ligand, and are susceptible to false positives. Thus, important information about the functional state of protein-ligand complexes cannot be obtained directly. Here we report a functional single-molecule binding assay that uses force spectroscopy to directly probe the functional consequence of ligand binding and report the functional state of protein-ligand complexes. As a proof of principle, we used protein G and the Fc fragment of IgG as a model system in this study. Binding of Fc to protein G does not induce major structural changes in protein G but results in significant enhancement of its mechanical stability. Using mechanical stability of protein G as an intrinsic functional reporter, we directly distinguished and quantified Fc-bound and Fc-free forms of protein G on a single-molecule basis and accurately determined their dissociation constant. This single-molecule functional binding assay is label-free, nearly background-free, and can detect functional heterogeneity, if any, among protein-ligand interactions. This methodology opens up avenues for studying protein-ligand interactions in a functional context, and we anticipate that it will find broad application in diverse protein-ligand systems.
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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.