ArticleProceedings of the National Academy of Sciences of the United States of America2013
High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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.
- Structural heterogeneity of iron-sulfur cluster scaffold protein IscU: Metamorphic or partially folded?Structural dynamics (Melville, N.Y.) · 2026Review
- Conformational landscapes of rigid and flexible molecules explored with variable temperature ion mobility-mass spectrometry.Nature communications · 2025Article
- Extremophilic hemoglobins: The structure of Shewanella benthica truncated hemoglobin N.The Journal of biological chemistry · 2025Article
- Heat and cold denaturation of yeast frataxin: The effect of pressure.Biophysical journal · 2022Article
- Transition-State Compressibility and Activation Volume of Transient Protein Conformational Fluctuations.JACS Au · 2021Article
- Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways.Molecules (Basel, Switzerland) · 2020Review
- The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth.PLoS computational biology · 2020Article
- Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- Combing Transcriptomes for Secrets of Deep-Sea Survival: Environmental Diversity Drives Patterns of Protein Evolution.Integrative and comparative biology · 2019Article
- 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
- Interrupted Pressure-Jump NMR Experiments Reveal Resonances of On-Pathway Protein Folding Intermediate.The journal of physical chemistry. B · 2018Article
- Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology.Methods (San Diego, Calif.) · 2018Article
- Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Simulated pressure denaturation thermodynamics of ubiquitin.Biophysical chemistry · 2017Article
- Computational investigation of cold denaturation in the Trp-cage miniprotein.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The energetics of a three-state protein folding system probed by high-pressure relaxation dispersion NMR spectroscopy.Angewandte Chemie (International ed. in English) · 2015Article
- The Complex Energy Landscape of the Protein IscU.Biophysical journal · 2015Article
- The hydrophobic temperature dependence of amino acids directly calculated from protein structures.PLoS computational biology · 2015Article
- "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
- Correlated parameter fit of arrhenius model for thermal denaturation of proteins and cells.Annals of biomedical engineering · 2014Article
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4 authors.
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Abstract
Proteins denature not only at high, but also at low temperature as well as high pressure. These denatured states are not easily accessible for experiment, because usually heat denaturation causes aggregation, whereas cold or pressure denaturation occurs at temperatures well below the freezing point of water or pressures above 5 kbar, respectively. Here we have obtained atomic details of the pressure-assisted, cold-denatured state of ubiquitin at 2,500 bar and 258 K by high-resolution NMR techniques. Under these conditions, a folded, native-like and a disordered state exist in slow exchange. Secondary chemical shifts show that the disordered state has structural propensities for a native-like N-terminal β-hairpin and α-helix and a nonnative C-terminal α-helix. These propensities are very similar to the previously described alcohol-denatured (A-)state. Similar to the A-state, (15)N relaxation data indicate that the secondary structure elements move as independent segments. The close similarity of pressure-assisted, cold-denatured, and alcohol-denatured states with native and nonnative secondary elements supports a hierarchical mechanism of folding and supports the notion that similar to alcohol, pressure and cold reduce the hydrophobic effect. Indeed, at nondenaturing concentrations of methanol, a complete transition from the native to the A-state can be achieved at ambient temperature by varying the pressure from 1 to 2,500 bar. The methanol-assisted pressure transition is completely reversible and can also be induced in protein G. This method should allow highly detailed studies of protein-folding transitions in a continuous and reversible manner.
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