ArticleBiophysical journal2007
A water-explicit lattice model of heat-, cold-, and pressure-induced protein unfolding.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Allostery without Conformational Change: A Native Mass Spectrometry Perspective.The journal of physical chemistry. B · 2025Article
- Hydrophobic Homopolymer's Coil-Globule Transition and Adsorption onto a Hydrophobic Surface under Different Conditions.The journal of physical chemistry. B · 2023Article
- Implicit water model within the Zimm-Bragg approach to analyze experimental data for heat and cold denaturation of proteins.Communications chemistry · 2021Article
- Temperature-Controlled Liquid-Liquid Phase Separation of Disordered Proteins.ACS central science · 2019Article
- Computational investigation of cold denaturation in the Trp-cage miniprotein.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A coarse-grained protein model in a water-like solvent.Scientific reports · 2013Article
- Understanding the role of hydrogen bonds in water dynamics and protein stability.Journal of biological physics · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
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Abstract
We investigate the effect of temperature and pressure on polypeptide conformational stability using a two-dimensional square lattice model in which water is represented explicitly. The model captures many aspects of water thermodynamics, including the existence of density anomalies, and we consider here the simplest representation of a protein: a hydrophobic homopolymer. We show that an explicit treatment of hydrophobic hydration is sufficient to produce cold, pressure, and thermal denaturation. We investigate the effects of the enthalpic and entropic components of the water-protein interactions on the overall folding phase diagram, and show that even a schematic model such as the one we consider yields reasonable values for the temperature and pressure ranges within which highly compact homopolymer configurations are thermodynamically stable.
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