ArticleBiophysical journal2010
High-pressure SAXS study of folded and unfolded ensembles of proteins.
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 14 papers.
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Who cites it
14 citing papers in PubMed, 47 citations in OpenAlex.
- Functionally related internal fluctuations in human ileal bile acid-binding protein by high pressure nuclear magnetic resonance.Protein science : a publication of the Protein Society · 2026Article
- Loosely-packed dynamical structures with partially-melted surface being the key for thermophilic argonaute proteins achieving high DNA-cleavage activity.Nucleic acids research · 2022Article
- Article
- Probing the existence of non-thermal Terahertz radiation induced changes of the protein solution structure.Scientific reports · 2021Article
- Thermodynamic stability of hnRNP A1 low complexity domain revealed by high-pressure NMR.Proteins · 2021Article
- Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1.Biophysical journal · 2020Article
- New insights into human hair: SAXS, SEM, TEM and EDX for Alopecia Areata investigations.PeerJ · 2020Article
- Lessons from pressure denaturation of proteins.Journal of the Royal Society, Interface · 2018Review
- High Hydrostatic Pressure Induces a Lipid Phase Transition and Molecular Rearrangements in Low-Density Lipoprotein Nanoparticles.Particle & particle systems characterization : measurement and description of particle properties and behavior in powders and other disperse systems · 2018Article
- A hypothesis to reconcile the physical and chemical unfolding of proteins.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Review
- Thermodynamic and functional characteristics of deep-sea enzymes revealed by pressure effects.Extremophiles : life under extreme conditions · 2013Review
- Measurement of energy landscape roughness of folded and unfolded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Revealing conformational substates of lipidated N-Ras protein by pressure modulation.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A structural interpretation of the thermodynamic stability of proteins requires an understanding of the structural properties of the unfolded state. High-pressure small-angle x-ray scattering was used to measure the effects of temperature, pressure, denaturants, and stabilizing osmolytes on the radii of gyration of folded and unfolded state ensembles of staphylococcal nuclease. A set of variants with the internal Val-66 replaced with Ala, Tyr, or Arg was used to examine how changes in the volume and polarity of an internal microcavity affect the dimensions of the native state and the pressure sensitivity of the ensemble. The unfolded state ensembles achieved for these proteins with high pressure were more compact than those achieved at high temperature, and were all very sensitive to the presence of urea and glycerol. Substitutions at the hydrophobic core detectably altered the conformation of the protein, even in the folded state. The introduction of a charged residue, such as Arg, inside the hydrophobic interior of a protein could dramatically alter the structural properties, even those of the unfolded state. The data suggest that a charge at an internal position can interfere with the formation of transient hydrophobic clusters in the unfolded state, and ensure that the pressure-unfolded form of a protein occupies the maximum volume possible. Only at high temperatures does the radius of gyration of the unfolded state ensemble approach the value for a statistical random coil.
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Registered trials
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