Consistent treatment of hydrophobicity in protein lattice models accounts for cold denaturation

Abstract

The hydrophobic effect stabilizes the native structure of proteins by minimizing the unfavourable 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.

Added and corrected references for design procedure in main text (p. 2) and in Supplemental Information (p. 8)

References in corpus (4)

• Microscopic mechanism for cold denaturation
• Generic Mechanism of Emergence of Amyloid Protofilaments from Disordered Oligomeric aggregates
• Contribution of Water to Pressure and Cold Denaturation of Proteins
• Interplay between folding and assembly of fibril-forming polypeptides

Cited by in corpus (5)

• In silico evidence that protein unfolding is as a precursor of the protein aggregation
• A Tale of Two Desolvation Potentials: An Investigation of Protein Behavior Under High Hydrostatic Pressure
• Lattice protein design using Bayesian learning
• The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth
• Introduction to Protein Structure Prediction