ArticleNature communications2017
An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed.
- Advances and opportunities for computational interrogation of plant proteins.The Plant journal : for cell and molecular biology · 2026Review
- Simulating Crowding In Vitro: Not an Elusive Goal Any Longer.Sub-cellular biochemistry · 2025Review
- Molecular Crowding: The History and Development of a Scientific Paradigm.Chemical reviews · 2024Review
- Temperature activated transient receptor potential ion channels from Antarctic fishes.Open biology · 2023Article
- Contrasting Changes in Strongly and Weakly Bound Hydration Water of a Protein upon Denaturation.The journal of physical chemistry. B · 2023Article
- Revitalizing an important field in biophysics: The new frontiers of molecular crowding.Frontiers in molecular biosciences · 2023Article
- The Protein Unfolded State: One, No One and One Hundred Thousand.Journal of the American Chemical Society · 2022Review
- Crowding-induced protein destabilization in the absence of soft attractions.Biophysical journal · 2022Article
- Recipes for Inducing Cold Denaturation in an Otherwise Stable Protein.Journal of the American Chemical Society · 2022Article
- Heat and cold denaturation of yeast frataxin: The effect of pressure.Biophysical journal · 2022Article
- From Protein Design to the Energy Landscape of a Cold Unfolding Protein.The journal of physical chemistry. B · 2022Article
- Protein Mutations and Stability, a Link with Disease: The Case Study of Frataxin.Biomedicines · 2022Review
- The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy.Communications chemistry · 2021Article
- The Stability Landscape of de novo TIM Barrels Explored by a Modular Design Approach.Journal of molecular biology · 2021Article
- Quantifying the thermodynamics of protein unfolding using 2D NMR spectroscopy.Communications chemistry · 2020Article
- Human Serum Albumin in the Presence of AGuIX Nanoagents: Structure Stabilisation without Direct Interaction.International journal of molecular sciences · 2020Article
- Insights on protein thermal stability: a graph representation of molecular interactions.Bioinformatics (Oxford, England) · 2019Article
- ProgrammingChemical science · 2019Article
- Melting Down Protein Stability: PAPS Synthase 2 in Patients and in a Cellular Environment.Frontiers in molecular biosciences · 2019Review
- The cold denaturation of IscU highlights structure-function dualism in marginally stable proteins.Communications chemistry · 2018Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Macromolecular crowding ought to stabilize folded forms of proteins, through an excluded volume effect. This explanation has been questioned and observed effects attributed to weak interactions with other cell components. Here we show conclusively that protein stability is affected by volume exclusion and that the effect is more pronounced when the crowder's size is closer to that of the protein under study. Accurate evaluation of the volume exclusion effect is made possible by the choice of yeast frataxin, a protein that undergoes cold denaturation above zero degrees, because the unfolded form at low temperature is more expanded than the corresponding one at high temperature. To achieve optimum sensitivity to changes in stability we introduce an empirical parameter derived from the stability curve. The large effect of PEG 20 on cold denaturation can be explained by a change in water activity, according to Privalov's interpretation of cold denaturation.
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Registered trials
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