ArticleEuropean biophysics journal : EBJ2006
Combined NMR-observation of cold denaturation in supercooled water and heat denaturation enables accurate measurement of deltaC(p) of protein unfolding.
Article in European biophysics journal : EBJ, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 45 citations in OpenAlex.
- Simulating Crowding In Vitro: Not an Elusive Goal Any Longer.Sub-cellular biochemistry · 2025Review
- Cooperative Conformational Transitions Underpin the Activation Heat Capacity in the Temperature Dependence of Enzyme Catalysis.ACS catalysis · 2024Article
- Fused in sarcoma undergoes cold denaturation: Implications for phase separation.Protein science : a publication of the Protein Society · 2023Article
- Recipes for Inducing Cold Denaturation in an Otherwise Stable Protein.Journal of the American Chemical Society · 2022Article
- Monitoring protein unfolding transitions by NMR-spectroscopy.Journal of biomolecular NMR · 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
- All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy.Nature communications · 2020Article
- Insight into the Folding and Dimerization Mechanisms of the N-Terminal Domain from Human TDP-43.International journal of molecular sciences · 2020Article
- Quantifying the thermodynamics of protein unfolding using 2D NMR spectroscopy.Communications chemistry · 2020Article
- Hydration shell differentiates folded and disordered states of a Trp-cage miniprotein, allowing characterization of structural heterogeneity by wide-line NMR measurements.Scientific reports · 2019Article
- The cold denaturation of IscU highlights structure-function dualism in marginally stable proteins.Communications chemistry · 2018Article
- An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states.Nature communications · 2017Article
- Article
- Water Determines the Structure and Dynamics of Proteins.Chemical reviews · 2016Review
- Cold denaturation as a tool to measure protein stability.Biophysical chemistry · 2016Review
- "Invisible" conformers of an antifungal disulfide protein revealed by constrained cold and heat unfolding, CEST-NMR experiments, and molecular dynamics calculations.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- NMR-based structural biology of proteins in supercooled water.Journal of structural and functional genomics · 2011Review
- The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structure.Journal of the American Chemical Society · 2010Article
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Authors and funding
4 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cold and heat denaturation of the double mutant Arg 3-->Glu/Leu 66-->Glu of cold shock protein Csp of Bacillus caldolyticus was monitored using 1D (1)H NMR spectroscopy in the temperature range from -12 degrees C in supercooled water up to +70 degrees C. The fraction of unfolded protein, f (u), was determined as a function of the temperature. The data characterizing the unfolding transitions could be consistently interpreted in the framework of two-state models: cold and heat denaturation temperatures were determined to be -11 degrees C and 39 degrees C, respectively. A joint fit to both cold and heat transition data enabled the accurate spectroscopic determination of the heat capacity difference between native and denatured state, DeltaC(p) of unfolding. The approach described in this letter, or a variant thereof, is generally applicable and promises to be of value for routine studies of protein folding.
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