ArticleJournal of the American Chemical Society2011
Size and sequence and the volume change of protein folding.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Does a Similar 3D Structure Mean a Similar Folding Pathway? The Presence of a C-TerminalMolecules (Basel, Switzerland) · 2023Article
- Review
- Heat and cold denaturation of yeast frataxin: The effect of pressure.Biophysical journal · 2022Article
- The Right-Handed Parallel β-Helix Topology ofBiomolecules · 2021Article
- Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR.Biology · 2021Article
- Thermodynamic stability of hnRNP A1 low complexity domain revealed by high-pressure NMR.Proteins · 2021Article
- Structure elucidation of the elusive Enzyme I monomer reveals the molecular mechanisms linking oligomerization and enzymatic activity.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Pressure and Chemical Unfolding of an α-Helical Bundle Protein: The GH2 Domain of the Protein Adaptor GIPC1.International journal of molecular sciences · 2021Article
- Molecular insights on poly(Physical chemistry chemical physics : PCCP · 2021Article
- Volume and compressibility differences between protein conformations revealed by high-pressure NMR.Biophysical journal · 2021Article
- Combining High-Pressure Perturbation with NMR Spectroscopy for a Structural and Dynamical Characterization of Protein Folding Pathways.Molecules (Basel, Switzerland) · 2020Review
- Folding of the Ig-Like Domain of the Dengue Virus Envelope Protein Analyzed by High-Hydrostatic-Pressure NMR at a Residue-Level Resolution.Biomolecules · 2019Article
- Lessons from pressure denaturation of proteins.Journal of the Royal Society, Interface · 2018Review
- Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology.Methods (San Diego, Calif.) · 2018Article
- Monitoring Unfolding of Titin I27 Single and Bi Domain with High-Pressure NMR Spectroscopy.Biophysical journal · 2018Article
- High-Pressure NMR and SAXS Reveals How Capping Modulates Folding Cooperativity of the pp32 Leucine-rich Repeat Protein.Journal of molecular biology · 2018Article
- Excess Volumes from the Pressure Derivative of the Excess Chemical Potential: Testing Simple Models for Cavity Formation in Water.ACS omega · 2017Article
- High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape.Biophysical journal · 2016Article
- Evolution under Drug Pressure Remodels the Folding Free-Energy Landscape of Mature HIV-1 Protease.Journal of molecular biology · 2016Article
- Silk-based stabilization of biomacromolecules.Journal of controlled release : official journal of the Controlled Release Society · 2015Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The application of hydrostatic pressure generally leads to protein unfolding, implying, in accordance with Le Chatelier's principle, that the unfolded state has a smaller molar volume than the folded state. However, the origin of the volume change upon unfolding, ΔV(u), has yet to be determined. We have examined systematically the effects of protein size and sequence on the value of ΔV(u) using as a model system a series of deletion variants of the ankyrin repeat domain of the Notch receptor. The results provide strong evidence in support of the notion that the major contributing factor to pressure effects on proteins is their imperfect internal packing in the folded state. These packing defects appear to be specifically localized in the 3D structure, in contrast to the uniformly distributed effects of temperature and denaturants that depend upon hydration of exposed surface area upon unfolding. Given its local nature, the extent to which pressure globally affects protein structure can inform on the degree of cooperativity and long-range coupling intrinsic to the folded state. We also show that the energetics of the protein's conformations can significantly modulate their volumetric properties, providing further insight into protein stability.
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