ArticleNature protocols2013
Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy.
Article in Nature protocols, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Force-Triggered Thermodynamically Uphill Disulfide Reduction through Sulfur Oxidation State Control.Journal of the American Chemical Society · 2025Article
- Single-molecule magnetic tweezers to unravel protein folding dynamics under force.Biophysical reviews · 2025Review
- FimH-mannose noncovalent bonds survive minutes to hours under force.Biophysical journal · 2024Article
- The strongest protein binder is surprisingly labile.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
- Structural anisotropy results in mechano-directional transport of proteins across nuclear pores.Nature physics · 2024Article
- Time-dependent extracellular matrix alterations of young tendons in response to stress relaxation: a model for the Ponseti method.Journal of the Royal Society, Interface · 2023Article
- Interdomain Linker Effect on the Mechanical Stability of Ig Domains in Titin.International journal of molecular sciences · 2022Article
- Nonexponential kinetics captured in sequential unfolding of polyproteins over a range of loads.Current research in structural biology · 2022Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Nanomechanical Phenotypes in Cardiac Myosin-Binding Protein C Mutants That Cause Hypertrophic Cardiomyopathy.ACS nano · 2021Article
- Regulation of titin-based cardiac stiffness by unfolded domain oxidation (UnDOx).Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A HaloTag-TEV genetic cassette for mechanical phenotyping of proteins from tissues.Nature communications · 2020Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- An Abl-FBP17 mechanosensing system couples local plasma membrane curvature and stress fiber remodeling during mechanoadaptation.Nature communications · 2019Article
- Multiplexed protein force spectroscopy reveals equilibrium protein folding dynamics and the low-force response of von Willebrand factor.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The mechanical stability of proteins regulates their translocation rate into the cell nucleus.Nature physics · 2019Article
- Redox regulation of protein nanomechanics in health and disease: Lessons from titin.Redox biology · 2019Review
- The extracellular matrix-myosin pathway in mechanotransduction: from molecule to tissue.Emerging topics in life sciences · 2018Article
- Force-Clamp Rheometry for Characterizing Protein-based Hydrogels.Journal of visualized experiments : JoVE · 2018Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Here we describe a protocol for using force-clamp spectroscopy to precisely quantify the effect of force on biochemical reactions. A calibrated force is used to control the exposure of reactive sites in a single polyprotein substrate composed of repeated domains. The use of polyproteins allows the identification of successful single-molecule recordings from unambiguous mechanical unfolding fingerprints. Biochemical reactions are then measured directly by detecting the length changes of the substrate held at a constant force. We present the layout of a force-clamp spectrometer along with protocols to design and conduct experiments. These experiments measure reaction kinetics as a function of applied force. We show sample data of the force dependency of two different reactions, protein unfolding and disulfide reduction. These data, which can be acquired in just a few days, reveal mechanistic details of the reactions that currently cannot be resolved by any other technique.
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