ArticleProceedings of the National Academy of Sciences of the United States of America2019
Ephemeral states in protein folding under force captured with a magnetic tweezers design.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Protein force spectroscopy using magnetic tweezers: Slow and steady wins the race?Biophysical journal · 2026Review
- Development of electromagnetic tweezers for single-molecule energetics of kinesin.Biophysics and physicobiology · 2026Article
- Force writes memory: proline isomerization as a molecular memory switch.Biochemical Society transactions · 2025Review
- Mechanical forces and ligand binding modulateLife science alliance · 2025Article
- Single-molecule magnetic tweezers to unravel protein folding dynamics under force.Biophysical reviews · 2025Review
- An accurate probabilistic step finder for time-series analysis.Biophysical journal · 2024Article
- Force-regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ.Protein science : a publication of the Protein Society · 2024Article
- Single-molecule magnetic tweezers to probe the equilibrium dynamics of individual proteins at physiologically relevant forces and timescales.Nature protocols · 2024Review
- Identical sequences, different behaviors: Protein diversity captured at the single-molecule level.Biophysical journal · 2024Article
- ForceGen: End-to-end de novo protein generation based on nonlinear mechanical unfolding responses using a language diffusion model.Science advances · 2024Article
- Article
- An accurate probabilistic step finder for time-series analysis.bioRxiv : the preprint server for biology · 2023Article
- Allosteric activation of vinculin by talin.Nature communications · 2023Article
- The Actin Network Interfacing Diverse Integrin-Mediated Adhesions.Biomolecules · 2023Review
- Single-molecule mechanical studies of chaperones and their clients.Biophysics reviews · 2022Review
- Mechanical regulation of talin through binding and history-dependent unfolding.Science advances · 2022Article
- Nano-Precision Tweezers for Mechanosensitive Proteins and Beyond.Molecules and cells · 2022Review
- The biophysics of cancer: emerging insights from micro- and nanoscale tools.Advanced nanobiomed research · 2022Article
- Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein.Communications chemistry · 2021Article
- Force spectroscopy with electromagnetic tweezers.Journal of applied physics · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Magnetic tape heads are ubiquitously used to read and record on magnetic tapes in technologies as diverse as old VHS tapes, modern hard-drive disks, or magnetic bands on credit cards. Their design highlights the ability to convert electric signals into fluctuations of the magnetic field at very high frequencies, which is essential for the high-density storage demanded nowadays. Here, we twist this conventional use of tape heads to implement one in a magnetic tweezers design, which offers the unique capability of changing the force with a bandwidth of ∼10 kHz. We calibrate our instrument by developing an analytical expression that predicts the magnetic force acting on a superparamagnetic bead based on the Karlqvist approximation of the magnetic field created by a tape head. This theory is validated by measuring the force dependence of protein L unfolding/folding step sizes and the folding properties of the R3 talin domain. We demonstrate the potential of our instrument by carrying out millisecond-long quenches to capture the formation of the ephemeral molten globule state in protein L, which has never been observed before. Our instrument provides the capability of interrogating individual molecules under fast-changing forces with a control and resolution below a fraction of a piconewton, opening a range of force spectroscopy protocols to study protein dynamics under force.
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Registered trials
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