ArticleBiophysical journal2007
Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of I27 and ubiquitin.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 136 citations in OpenAlex.
- The local mechanostructural properties of protein cargoes regulate nucleocytoplasmic transport.Nature physics · 2026Article
- Structural Basis of High-Precision Protein Ligation and Its Application.Journal of the American Chemical Society · 2025Article
- Structural anisotropy results in mechano-directional transport of proteins across nuclear pores.Nature physics · 2024Article
- Nonexponential kinetics captured in sequential unfolding of polyproteins over a range of loads.Current research in structural biology · 2022Article
- Molecular Fluctuations as a Ruler of Force-Induced Protein Conformations.Nano letters · 2021Article
- FliIScientific reports · 2020Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
- Enzymatic biosynthesis and immobilization of polyprotein verified at the single-molecule level.Nature communications · 2019Article
- Conformational entropy of a single peptide controlled under force governs protease recognition and catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Reducing uncertainties in energy dissipation measurements in atomic force spectroscopy of molecular networks and cell-adhesion studies.Scientific reports · 2018Article
- The force-dependent mechanism of DnaK-mediated mechanical folding.Science advances · 2018Article
- Warhammers for Peaceful Times.Biophysical journal · 2018Article
- Protein S-sulfenylation is a fleeting molecular switch that regulates non-enzymatic oxidative folding.Nature communications · 2016Article
- Mechanical Folding and Unfolding of Protein Barnase at the Single-Molecule Level.Biophysical journal · 2016Article
- Titin domains progressively unfolded by force are homogenously distributed along the molecule.Biophysical journal · 2015Article
- Dynamics of equilibrium folding and unfolding transitions of titin immunoglobulin domain under constant forces.Journal of the American Chemical Society · 2015Article
- Unraveling the mysteries of chaperone interactions of the myosin head.Biophysical journal · 2014Article
- Identification of allosteric disulfides from prestress analysis.Biophysical journal · 2014Article
- Nanomechanics of HaloTag tethers.Journal of the American Chemical Society · 2013Article
- Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.Methods (San Diego, Calif.) · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Single-protein force experiments have relied on a molecular fingerprint based on tethering multiple single-protein domains in a polyprotein chain. However, correlations between these domains remain an issue in interpreting force spectroscopy data, particularly during protein folding. Here we first show that force-clamp spectroscopy is a sensitive technique that provides a molecular fingerprint based on the unfolding step size of four single-monomer proteins. We then measure the force-dependent unfolding rate kinetics of ubiquitin and I27 monomers and find a good agreement with the data obtained for the respective polyproteins over a wide range of forces, in support of the Markovian hypothesis. Moreover, with a large statistical ensemble at a single force, we show that ubiquitin monomers also exhibit a broad distribution of unfolding times as a signature of disorder in the folded protein landscape. Furthermore, we readily capture the folding trajectories of monomers that exhibit the same stages in folding observed for polyproteins, thus eliminating the possibility of entropic masking by other unfolded modules in the chain or domain-domain interactions. On average, the time to reach the I27 folded length increases with increasing quenching force at a rate similar to that of the polyproteins. Force-clamp spectroscopy at the single-monomer level reproduces the kinetics of unfolding and refolding measured using polyproteins, which proves that there is no mechanical effect of tethering proteins to one another in the case of ubiquitin and I27.
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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.