ArticleBiophysical journal2006
Heteropolymer collapse theory for protein folding in the pressure-temperature plane.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
9 citing papers in PubMed.
- Review
- Behavior of Proteins under Pressure from Experimental Pressure-Dependent Structures.The journal of physical chemistry. B · 2021Article
- A Tale of Two Desolvation Potentials: An Investigation of Protein Behavior under High Hydrostatic Pressure.The journal of physical chemistry. B · 2020Article
- High pressure inhibits signaling protein binding to the flagellar motor and bacterial chemotaxis through enhanced hydration.Scientific reports · 2020Article
- Temperature-Controlled Liquid-Liquid Phase Separation of Disordered Proteins.ACS central science · 2019Article
- Role of solvation in pressure-induced helix stabilization.The Journal of chemical physics · 2014Article
- Temperature and pressure dependence of protein stability: the engineered fluorescein-binding lipocalin FluA shows an elliptic phase diagram.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- A water-explicit lattice model of heat-, cold-, and pressure-induced protein unfolding.Biophysical journal · 2007Article
- Coarse-grained strategy for modeling protein stability in concentrated solutions. III: directional protein interactions.Biophysical journal · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We revisit a heteropolymer collapse theory originally introduced to explore how the balance between hydrophobic interactions and configurational entropy determines the thermal stability of globular proteins at ambient pressure. We generalize the theory by introducing a basic statistical mechanical treatment for how pressure impacts the solvent-mediated interactions between hydrophobic amino-acid residues. In particular, we estimate the strength of the hydrophobic interactions using a molecular thermodynamic model for the interfacial free energy between liquid water and a curved hydrophobic solute. The model, which also reproduces many of the distinctive thermodynamic properties of aqueous solutions in bulk and interfacial environments, predicts that the water-solute interfacial free energy is significantly reduced by the application of high hydrostatic pressures. This allows water to penetrate into folded heteropolymers at high pressure and break apart their hydrophobic cores, a scenario suggested earlier by information theory calculations. As a result, folded heteropolymers are predicted to display the kind of closed region of stability in the pressure-temperature plane exhibited by native proteins. We compare predictions of the collapse theory with experimental data for several proteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.