ArticleProceedings of the National Academy of Sciences of the United States of America2015
On artifacts in single-molecule force spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Modeling Targeted Mechanochemistry in Polymeric Solids.Chemical reviews · 2026Review
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Massively parallel bead-free force spectroscopy with fluorescence.Science advances · 2026Article
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- A theoretical framework for random acceleration molecular dynamics simulations.The Journal of chemical physics · 2026Article
- Good Rates From Bad Coordinates: The Exponential Average Time-dependent Rate Approach.Journal of chemical theory and computation · 2024Article
- Identical sequences, different behaviors: Protein diversity captured at the single-molecule level.Biophysical journal · 2024Article
- Microscopic theory, analysis, and interpretation of conductance histograms in molecular junctions.Nature communications · 2023Article
- Nonlinear effects in optical trapping of titanium dioxide and diamond nanoparticles.Biophysical journal · 2023Article
- Robust membrane protein tweezers reveal the folding speed limit of helical membrane proteins.eLife · 2023Article
- Inferring equilibrium transition rates from nonequilibrium protocols.Biophysical journal · 2023Article
- The Effect of Time Resolution on Apparent Transition Path Times Observed in Single-Molecule Studies of Biomolecules.The journal of physical chemistry. B · 2022Article
- Nonexponential kinetics captured in sequential unfolding of polyproteins over a range of loads.Current research in structural biology · 2022Article
- Observing the base-by-base search for native structure along transition paths during the folding of single nucleic acid hairpins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Massively Parallelized Molecular Force Manipulation with On-Demand Thermal and Optical Control.Journal of the American Chemical Society · 2021Article
- Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein.Communications chemistry · 2021Article
- Energy landscapes of fast-folding proteins pushing the limits of atomic force microscope (AFM) pulling.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Molecular Fluctuations as a Ruler of Force-Induced Protein Conformations.Nano letters · 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
- Estimating transition path times and shapes from single-molecule photon trajectories: A simulation analysis.The Journal of chemical physics · 2021Article
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Authors and funding
3 authors.
Funding
Abstract
In typical force spectroscopy experiments, a small biomolecule is attached to a soft polymer linker that is pulled with a relatively large bead or cantilever. At constant force, the total extension stochastically changes between two (or more) values, indicating that the biomolecule undergoes transitions between two (or several) conformational states. In this paper, we consider the influence of the dynamics of the linker and mesoscopic pulling device on the force-dependent rate of the conformational transition extracted from the time dependence of the total extension, and the distribution of rupture forces in force-clamp and force-ramp experiments, respectively. For these different experiments, we derive analytic expressions for the observables that account for the mechanical response and dynamics of the pulling device and linker. Possible artifacts arise when the characteristic times of the pulling device and linker become comparable to, or slower than, the lifetimes of the metastable conformational states, and when the highly anharmonic regime of stretched linkers is probed at high forces. We also revisit the problem of relating force-clamp and force-ramp experiments, and identify a linker and loading rate-dependent correction to the rates extracted from the latter. The theory provides a framework for both the design and the quantitative analysis of force spectroscopy experiments by highlighting, and correcting for, factors that complicate their interpretation.
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