ArticleBiophysical journal2014
Determining intrachain diffusion coefficients for biopolymer dynamics from single-molecule force spectroscopy measurements.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Quantitative Elasticity of Flexible Polymer Chains Using Interferometer-Based AFM.Nanomaterials (Basel, Switzerland) · 2022Article
- 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
- 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
- Position-, disorder-, and salt-dependent diffusion in binding-coupled-folding of intrinsically disordered proteins.Physical chemistry chemical physics : PCCP · 2019Article
- 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
- 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
- Quantifying Instrumental Artifacts in Folding Kinetics Measured by Single-Molecule Force Spectroscopy.Biophysical journal · 2016Article
- Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein.Nature communications · 2016Article
- Article
- Mechanical Folding and Unfolding of Protein Barnase at the Single-Molecule Level.Biophysical journal · 2016Article
- Extracting intrinsic dynamic parameters of biomolecular folding from single-molecule force spectroscopy experiments.Protein science : a publication of the Protein Society · 2016Article
- On artifacts in single-molecule force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Optimizing 1-μs-Resolution Single-Molecule Force Spectroscopy on a Commercial Atomic Force Microscope.Nano letters · 2015Article
- Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Testing Landscape Theory for Biomolecular Processes with Single Molecule Fluorescence Spectroscopy.Physical review letters · 2015Article
- Reconstructing folding energy landscapes from splitting probability analysis of single-molecule trajectories.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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3 authors.
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Abstract
The conformational diffusion coefficient for intrachain motions in biopolymers, D, sets the timescale for structural dynamics. Recently, force spectroscopy has been applied to determine D both for unfolded proteins and for the folding transitions in proteins and nucleic acids. However, interpretation of the results remains unsettled. We investigated how instrumental effects arising from the force probes used in the measurement can affect the value of D recovered via force spectroscopy. We compared estimates of D for the folding of DNA hairpins found from measurements of rates and energy landscapes made using optical tweezers with estimates obtained from the same single-molecule trajectories via the transition path time. The apparent D obtained from the rates was much lower than the result found from the same data using transition time analysis, reflecting the effects of the mechanical properties of the force probe. Deconvolution of the finite compliance effects on the measurement allowed the intrinsic value to be recovered. These results were supported by Brownian dynamics simulations of the effects of force-probe compliance and bead size.
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