ArticleBiophysical journal2016
Quantifying Instrumental Artifacts in Folding Kinetics Measured by Single-Molecule Force Spectroscopy.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 39 citations in OpenAlex.
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- 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
- Quantitative Elasticity of Flexible Polymer Chains Using Interferometer-Based AFM.Nanomaterials (Basel, Switzerland) · 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
- 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
- Broad distributions of transition-path times are fingerprints of multidimensionality of the underlying free energy landscapes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Molecular free energy profiles from force spectroscopy experiments by inversion of observed committors.The Journal of chemical physics · 2019Article
- Mechanical unfolding of spectrin reveals a super-exponential dependence of unfolding rate on force.Scientific reports · 2019Article
- Measuring the average shape of transition paths during the folding of a single biological molecule.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Communication: Transition-path velocity as an experimental measure of barrier crossing dynamics.The Journal of chemical physics · 2018Article
- Probing Position-Dependent Diffusion in Folding Reactions Using Single-Molecule Force Spectroscopy.Biophysical journal · 2018Article
- Transition paths in single-molecule force spectroscopy.The Journal of chemical physics · 2018Article
- Transition Path Times Measured by Single-Molecule Spectroscopy.Journal of molecular biology · 2018Review
- The Work of Titin Protein Folding as a Major Driver in Muscle Contraction.Annual review of physiology · 2018Review
- Communication: Coordinate-dependent diffusivity from single molecule trajectories.The Journal of chemical physics · 2017Article
- Direct measurement of sequence-dependent transition path times and conformational diffusion in DNA duplex formation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Force spectroscopy is commonly used to measure the kinetics of processes occurring in single biological molecules. These measurements involve attaching the molecule of interest to micron-sized or larger force probes via compliant linkers. Recent theoretical work has described how the properties of the probes and linkers can alter the observed kinetics from the intrinsic behavior of the molecule in isolation. We applied this theory to estimate the errors in measurements of folding made using optical tweezers. Errors in the folding rates arising from instrument artifacts were only ∼20% for constant-force measurements of DNA hairpins with typical choices of linker length and probe size. Measurements of transition paths using a constant trap position at high trap stiffness were also found to be in the low-artifact limit. These results indicate that typical optical trap measurements of kinetics reflect the dynamics of the molecule fairly well, and suggest practical limitations on experimental design to ensure reliable kinetic measurements.
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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.