ArticleBiophysical journal2023
Temperature dependent mechanical unfolding and refolding of a protein studied by thermo-regulated optical tweezers.
Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Immunoglobulin binding protein (BiP) forms two types of dimers.Protein science : a publication of the Protein Society · 2026Article
- Single-molecule analysis reveals low-temperature misfolding in HIV-1 TAR RNA.Scientific reports · 2026Article
- A temperature-controlled chip holder with integrated electrodes for nanofluidic scattering spectroscopy on highly integrated nanofluidic systems.Microsystems & nanoengineering · 2026Article
- Materials and measurement in mechanobiology.Biophysical journal · 2025Article
- FAIR data for optical tweezers experiments.Biophysical journal · 2025Review
- On the free energy of protein folding in optical tweezers experiments.Biophysical reviews · 2025Review
- On the distance to the transition state of protein folding in optical tweezers experiments.Biophysical reviews · 2025Review
- Effect of temperature and nucleotide on the binding of BiP chaperone to a protein substrate.Protein science : a publication of the Protein Society · 2023Article
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Authors and funding
5 authors.
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Abstract
Temperature is a useful system variable to gather kinetic and thermodynamic information from proteins. Usually, free energy and the associated entropic and enthalpic contributions are obtained by quantifying the conformational equilibrium based on melting experiments performed in bulk conditions. Such experiments are suitable only for those small single-domain proteins whose side reactions of irreversible aggregation are unlikely to occur. Here, we avoid aggregation by pulling single-protein molecules in a thermo-regulated optical tweezers. Thus, we are able to explore the temperature dependence of the thermodynamic and kinetic parameters of MJ0366 from Methanocaldococcus jannaschii at the single-molecule level. By performing force-ramp experiments between 2°C and 40°C, we found that MJ0366 has a nonlinear dependence of free energy with temperature and a specific heat change of 2.3 ± 1.2 kcal/mol
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