ArticleThe Journal of biological chemistry2011
Direct quantification of the attempt frequency determining the mechanical unfolding of ubiquitin protein.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
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- Computational Prediction of the Complete Adsorption-Regeneration Cycle of Functionalized Metal-Organic Frameworks for Atmospheric Water Harvesting.ACS applied nano materials · 2026Article
- First-principles studies of the SClJournal of molecular modeling · 2025Article
- A Density Functional Theory (DFT) Perspective on Optical Absorption of Modified Graphene Interacting with the Main Amino Acids of Spider Silk.International journal of molecular sciences · 2023Article
- Measuring biological materials mechanics with atomic force microscopy - Mechanical unfolding of biopolymers.Microscopy research and technique · 2022Article
- Ab Initio Study of the Interaction of a Graphene Surface Decorated with a Metal-Doped CInternational journal of molecular sciences · 2022Article
- Direct observation of chaperone-modulated talin mechanics with single-molecule resolution.Communications biology · 2022Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Article
- Talin folding as the tuning fork of cellular mechanotransduction.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A modular DNA scaffold to study protein-protein interactions at single-molecule resolution.Nature nanotechnology · 2019Article
- Removal of a Conserved Disulfide Bond Does Not Compromise Mechanical Stability of a VHH Antibody Complex.Nano letters · 2019Article
- Probing Position-Dependent Diffusion in Folding Reactions Using Single-Molecule Force Spectroscopy.Biophysical journal · 2018Article
- Multidomain proteins under force.Nanotechnology · 2017Article
- Single-Molecule Protein Folding Experiments Using High-Precision Optical Tweezers.Methods in molecular biology (Clifton, N.J.) · 2017Article
- A HaloTag Anchored Ruler for Week-Long Studies of Protein Dynamics.Journal of the American Chemical Society · 2016Article
- Structure-Based Derivation of Protein Folding Intermediates and Energies from Optical Tweezers.Biophysical journal · 2016Article
- The role of binding site on the mechanical unfolding mechanism of ubiquitin.Scientific reports · 2015Article
- Determining intrachain diffusion coefficients for biopolymer dynamics from single-molecule force spectroscopy measurements.Biophysical journal · 2014Article
- How force unfolding differs from chemical denaturation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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3 authors.
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Abstract
Understanding protein dynamics requires a comprehensive knowledge of the underlying potential energy surface that governs the motion of each individual protein molecule. Single molecule mechanical studies have provided the unprecedented opportunity to study the individual unfolding pathways along a well defined coordinate, the end-to-end length of the protein. In these experiments, unfolding requires surmounting an energy barrier that separates the native from the extended state. The calculation of the absolute value of the barrier height has traditionally relied on the assumption of an attempt frequency, υ(‡). Here we used single molecule force-clamp spectroscopy to directly determine the value of υ(‡) for mechanical unfolding by measuring the unfolding rate of the small protein ubiquitin at varying temperatures. Our experiments demonstrate a significant effect of the temperature on the mechanical rate of unfolding. By extrapolating the unfolding rate in the absence of force for different temperatures, varying within the range spanning from 5 to 45 °C, we measured a value for the activation barrier of ΔG(‡) = 71 ± 5 kJ/mol and an exponential prefactor υ(‡) ∼4 × 10(9) s(-1). Although the measured prefactor value is 3 orders of magnitude smaller than the value predicted by the transition state theory (∼6 × 10(12) s(-1)), it is 400-fold higher than that encountered in analogous experiments studying the effect of temperature on the reactivity of a protein-embedded disulfide bond (∼10(7) M(-1) s(-1)). This approach will allow quantitative characterization of the complete energy landscape of a folding polypeptide from highly extended states, of capital importance for proteins with elastic function.
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