Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation

Erik van Dijk, Patrick Varilly, Tuomas P J Knowles, Daan Frenkel, Sanne Abeln

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The hydrophobic effect stabilizes the native structure of proteins by minimizing the unfavorable interactions between hydrophobic residues and water through the formation of a hydrophobic core. Here, we include the entropic and enthalpic contributions of the hydrophobic effect explicitly in an implicit solvent model. This allows us to capture two important effects: a length-scale dependence and a temperature dependence for the solvation of a hydrophobic particle. This consistent treatment of the hydrophobic effect explains cold denaturation and heat capacity measurements of solvated proteins.

Original languageEnglish
Pages (from-to)078101
JournalPhysical Review Letters
Volume116
Issue number7
DOIs
Publication statusPublished - 19 Feb 2016

Fingerprint

biopolymer denaturation
hydrophobicity
proteins
solvation
specific heat
temperature dependence
water
interactions

Keywords

  • Cold Temperature
  • Hydrophobic and Hydrophilic Interactions
  • Models, Chemical
  • Monte Carlo Method
  • Peptides
  • Protein Denaturation
  • Protein Folding
  • Proteins
  • Water
  • Journal Article
  • Research Support, Non-U.S. Gov't

Cite this

van Dijk, Erik ; Varilly, Patrick ; Knowles, Tuomas P J ; Frenkel, Daan ; Abeln, Sanne. / Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation. In: Physical Review Letters. 2016 ; Vol. 116, No. 7. pp. 078101.
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Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation. / van Dijk, Erik; Varilly, Patrick; Knowles, Tuomas P J; Frenkel, Daan; Abeln, Sanne.

In: Physical Review Letters, Vol. 116, No. 7, 19.02.2016, p. 078101.

Research output: Contribution to JournalArticleAcademicpeer-review

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AU - van Dijk, Erik

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AU - Frenkel, Daan

AU - Abeln, Sanne

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KW - Cold Temperature

KW - Hydrophobic and Hydrophilic Interactions

KW - Models, Chemical

KW - Monte Carlo Method

KW - Peptides

KW - Protein Denaturation

KW - Protein Folding

KW - Proteins

KW - Water

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

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