ArticleJournal of the American Chemical Society2015
Dynamics of equilibrium folding and unfolding transitions of titin immunoglobulin domain under constant forces.
Article in Journal of the American Chemical Society, 2015. 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.
- Using Magnetic Tweezers to Unravel the Mechanism of the G-Quadruplex Binding and Unwinding Activities of DHX36 Helicase.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Protein force spectroscopy using magnetic tweezers: Slow and steady wins the race?Biophysical journal · 2026Review
- Computational design of superstable proteins through maximized hydrogen bonding.Nature chemistry · 2026Article
- Effect of Additional Terminal Residues on the Folding and Unfolding Dynamics of Cold Shock Protein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The mechanical response of vinculin.Science advances · 2025Article
- Mechanochemistry: Fundamental Principles and Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Mechanically weak and highly dynamic state of mechanosensitive titin Ig domains induced by proline isomerization.Nature communications · 2025Article
- Single-molecule magnetic tweezers to unravel protein folding dynamics under force.Biophysical reviews · 2025Review
- Viscoelasticity of a single poly-protein probed step-by-step during its mechanical unfolding and refolding under the force-clamp conditions.RSC advances · 2025Article
- Pulling Forces Differentially Affect Refolding Pathways Due to Entangled Misfolded States in SARS-CoV-1 and SARS-CoV-2 Receptor Binding Domain.Biomolecules · 2024Article
- Single-molecule magnetic tweezers to probe the equilibrium dynamics of individual proteins at physiologically relevant forces and timescales.Nature protocols · 2024Review
- Structural domain in the Titin N2B-us region binds to FHL2 in a force-activation dependent manner.Nature communications · 2024Article
- Article
- Robust membrane protein tweezers reveal the folding speed limit of helical membrane proteins.eLife · 2023Article
- Ensemble Force Spectroscopy of a G-Quadruplex Cluster on a Single-Molecule Platform.Biomacromolecules · 2022Article
- Mechanical Stabilization of a Bacterial Adhesion Complex.Journal of the American Chemical Society · 2022Article
- A conformational transition of the D'D3 domain primes von Willebrand factor for multimerization.Blood advances · 2022Article
- Direct observation of chaperone-modulated talin mechanics with single-molecule resolution.Communications biology · 2022Article
- Advances in the Biological Application of Force-Induced Remnant Magnetization Spectroscopy.Molecules (Basel, Switzerland) · 2022Review
- Biophysical Approaches for Applying and Measuring Biological Forces.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Review
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Authors and funding
7 authors.
Funding
Abstract
The mechanical stability of force-bearing proteins is crucial for their functions. However, slow transition rates of complex protein domains have made it challenging to investigate their equilibrium force-dependent structural transitions. Using ultra stable magnetic tweezers, we report the first equilibrium single-molecule force manipulation study of the classic titin I27 immunoglobulin domain. We found that individual I27 in a tandem repeat unfold/fold independently. We obtained the force-dependent free energy difference between unfolded and folded I27 and determined the critical force (∼5.4 pN) at which unfolding and folding have equal probability. We also determined the force-dependent free energy landscape of unfolding/folding transitions based on measurement of the free energy cost of unfolding. In addition to providing insights into the force-dependent structural transitions of titin I27, our results suggest that the conformations of titin immunoglobulin domains can be significantly altered during low force, long duration muscle stretching.
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