ArticleProceedings of the National Academy of Sciences of the United States of America2019
Multiplexed protein force spectroscopy reveals equilibrium protein folding dynamics and the low-force response of von Willebrand factor.
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 46 papers.
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Who cites it
46 citing papers in PubMed, 94 citations in OpenAlex.
- MTERF1 polar roadblock mechanism revealed using high-throughput magnetic tweezers and accurate single-bead force calibration.Nucleic acids research · 2026Article
- Identification of missense variants in the C-domains of von Willebrand factor that cause gain-of-function-like activity.Blood advances · 2026Article
- Protein force spectroscopy using magnetic tweezers: Slow and steady wins the race?Biophysical journal · 2026Review
- Beyond the Single Molecule: Multiplexed Methods in Force Spectroscopy.Annual review of biophysics · 2026Review
- DNA twist at high alkali ion concentrations: evidence against C-form DNA in solution.Nucleic acids research · 2026Article
- Development of electromagnetic tweezers for single-molecule energetics of kinesin.Biophysics and physicobiology · 2026Article
- Article
- Mechanical forces and ligand binding modulateLife science alliance · 2025Article
- Single-molecule magnetic tweezers to unravel protein folding dynamics under force.Biophysical reviews · 2025Review
- Exploring force-driven stochastic folding dynamics in mechano-responsive proteins and implications in phenotypic variation.Nature communications · 2025Article
- Accurate drift-invariant single-molecule force calibration using the Hadamard variance.Biophysical journal · 2024Article
- FimH-mannose noncovalent bonds survive minutes to hours under force.Biophysical journal · 2024Article
- Cryptic Extensibility in von Willebrand Factor Revealed by Molecular Nanodissection.International journal of molecular sciences · 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
- Investigation of metal ion binding biomolecules one molecule at a time.Frontiers in chemistry · 2024Review
- High-yield ligation-free assembly of DNA constructs with nucleosome positioning sequence repeats for single-molecule manipulation assays.The Journal of biological chemistry · 2023Article
- Robust membrane protein tweezers reveal the folding speed limit of helical membrane proteins.eLife · 2023Article
- The intestinal MUC2 mucin C-terminus is stabilized by an extra disulfide bond in comparison to von Willebrand factor and other gel-forming mucins.Nature communications · 2023Article
- The role of single protein elasticity in mechanobiology.Nature reviews. Materials · 2023Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-molecule force spectroscopy has provided unprecedented insights into protein folding, force regulation, and function. So far, the field has relied primarily on atomic force microscope and optical tweezers assays that, while powerful, are limited in force resolution, throughput, and require feedback for constant force measurements. Here, we present a modular approach based on magnetic tweezers (MT) for highly multiplexed protein force spectroscopy. Our approach uses elastin-like polypeptide linkers for the specific attachment of proteins, requiring only short peptide tags on the protein of interest. The assay extends protein force spectroscopy into the low force (<1 pN) regime and enables parallel and ultra-stable measurements at constant forces. We present unfolding and refolding data for the small, single-domain protein ddFLN4, commonly used as a molecular fingerprint in force spectroscopy, and for the large, multidomain dimeric protein von Willebrand factor (VWF) that is critically involved in primary hemostasis. For both proteins, our measurements reveal exponential force dependencies of unfolding and refolding rates. We directly resolve the stabilization of the VWF A2 domain by Ca
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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.