ArticleBiophysical journal2010
Unique features of the folding landscape of a repeat protein revealed by pressure perturbation.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 43 citations in OpenAlex.
- Many Ways Out: Beyond the Two-State Model of Protein Unfolding.ACS omega · 2026Review
- Probing the structural stability of R-phycocyanin under pressure.Protein science : a publication of the Protein Society · 2024Article
- Protein-Ligand Binding Volume Determined from a Single 2D NMR Spectrum with Increasing Pressure.The journal of physical chemistry. B · 2021Article
- Lessons from pressure denaturation of proteins.Journal of the Royal Society, Interface · 2018Review
- High-Pressure NMR and SAXS Reveals How Capping Modulates Folding Cooperativity of the pp32 Leucine-rich Repeat Protein.Journal of molecular biology · 2018Article
- Molecular determinant of the effects of hydrostatic pressure on protein folding stability.Nature communications · 2017Article
- Transition state and ground state properties of the helix-coil transition in peptides deduced from high-pressure studies.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Model-independent decomposition of two-state data.Physical review. E, Statistical, nonlinear, and soft matter physics · 2013Article
- Misplaced helix slows down ultrafast pressure-jump protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Volume of Hsp90 ligand binding and the unfolding phase diagram as a function of pressure and temperature.European biophysics journal : EBJ · 2013Article
- 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
- Size and sequence and the volume change of protein folding.Journal of the American Chemical Society · 2011Article
- Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH.Proteins · 2011Article
- The folding of single domain proteins--have we reached a consensus?Current opinion in structural biology · 2011Review
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
The volumetric properties of proteins yield information about the changes in packing and hydration between various states along the folding reaction coordinate and are also intimately linked to the energetics and dynamics of these conformations. These volumetric characteristics can be accessed via pressure perturbation methods. In this work, we report high-pressure unfolding studies of the ankyrin domain of the Notch receptor (Nank1-7) using fluorescence, small-angle x-ray scattering, and Fourier transform infrared spectroscopy. Both equilibrium and pressure-jump kinetic fluorescence experiments were consistent with a simple two-state folding/unfolding transition under pressure, with a rather small volume change for unfolding compared to proteins of similar molecular weight. High-pressure fluorescence, Fourier transform infrared spectroscopy, and small-angle x-ray scattering measurements revealed that increasing urea over a very small range leads to a more expanded pressure unfolded state with a significant decrease in helical content. These observations underscore the conformational diversity of the unfolded-state basin. The temperature dependence of pressure-jump fluorescence relaxation measurements demonstrated that at low temperatures, the folding transition state ensemble (TSE) lies close in volume to the folded state, consistent with significant dehydration at the barrier. In contrast, the thermal expansivity of the TSE was found to be equivalent to that of the unfolded state, indicating that the interactions that constrain the folded-state thermal expansivity have not been established at the folding barrier. This behavior reveals a high degree of plasticity of the TSE of Nank1-7.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.