ArticleBiopolymers2017
Hydrophobic-hydrophilic forces in protein folding.
Article in Biopolymers, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Proteins Inside the HSP60/HSP10 Fold Under a Constant Electric Field: Potential Implications for the Protein Folding Problem.International journal of molecular sciences · 2026Article
- Properties Governing Native State Entanglements and Relationships to Protein Function.Journal of molecular biology · 2025Article
- Influence of 2-hydroxyethylammonium acetate-based protic ionic liquids on the thermophysical properties of aqueous DL-alanine solutions.BMC chemistry · 2025Article
- Isoleucine Binding and Regulation ofBiochemistry · 2025Article
- Accurate quantum-centric simulations of intermolecular interactions.Communications physics · 2025Article
- Article
- Molecular, structural, and functional characterization of delta subunit of T-complex protein-1 fromInfection and immunity · 2024Article
- Influence of the Water Model on the Structure and Interactions of the GPR40 Protein with the Lipid Membrane and the Solvent: Rigid versus Flexible Water Models.Journal of chemical theory and computation · 2024Article
- ARIP: A Tool for Precise Interatomic Contact Area and Volume Calculation in Proteins.International journal of molecular sciences · 2024Article
- Electrical Fields in the Processing of Protein-Based Foods.Foods (Basel, Switzerland) · 2024Review
- Revealing the mechanism of the lutein protective function of epicatechin-fructan glycosylated soybean protein isolate.Current research in food science · 2024Article
- Intelligent Protein Design and Molecular Characterization Techniques: A Comprehensive Review.Molecules (Basel, Switzerland) · 2023Review
- Ordered-domain unfolding of thermophilic isolated β subunit ATP synthase.Protein science : a publication of the Protein Society · 2023Article
- From Protein Design to the Energy Landscape of a Cold Unfolding Protein.The journal of physical chemistry. B · 2022Article
- Contribution of hydrophobic interactions to protein mechanical stability.Computational and structural biotechnology journal · 2022Article
- Temperature Dependence of Hydrophobic and Hydrophilic Forces and Interactions.The journal of physical chemistry. B · 2021Article
- Protein Surface Interactions-Theoretical and Experimental Studies.Frontiers in molecular biosciences · 2021Review
- Changes of Conformation in Albumin with Temperature by Molecular Dynamics Simulations.Entropy (Basel, Switzerland) · 2020Article
- Theoretical analysis on thermodynamic stability of chignolin.Scientific reports · 2019Article
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2 authors.
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Abstract
The process of protein folding is obviously driven by forces exerted on the atoms of the amino-acid chain. These forces arise from interactions with other parts of the protein itself (direct forces), as well as from interactions with the solvent (solvent-induced forces). We present a statistical-mechanical formalism that describes both these direct and indirect, solvent-induced thermodynamic forces on groups of the protein. We focus on 2 kinds of protein groups, commonly referred to as hydrophobic and hydrophilic. Analysis of this result leads to the conclusion that the forces on hydrophilic groups are in general stronger than on hydrophobic groups. This is then tested and verified by a series of molecular dynamics simulations, examining both hydrophobic alkanes of different sizes and hydrophilic moieties represented by polar-neutral hydroxyl groups. The magnitude of the force on assemblies of hydrophilic groups is dependent on their relative orientation: with 2 to 4 times larger forces on groups that are able to form one or more direct hydrogen bonds.
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