Jump to main content
Jump to site search

Issue 22, 2012
Previous Article Next Article

Thermal stability limits of proteins in solution and adsorbed on a hydrophobic surface

Author affiliations

Abstract

A coarse-grained Monte Carlo simulation is used to study thermal denaturation of small proteins in an infinitely dilute solution and adsorbed on a flat hydrophobic surface. Intermolecular interactions are modeled using the Miyazawa–Jernigan (MJ) knowledge-based potential for implicit solvent with the BULDG hydrophobicity scale. We analyze the thermal behavior of lysozyme for its prevalence of α-helices, fibronectin for its prevalence of β-sheets, and a short single helical peptide. Protein dimensions and contact maps are studied in detail before and during isothermal adsorption and heating. The MJ potential is shown to correctly predict the native conformation in solution under standard conditions, and the anticipated thermal stabilization of adsorbed proteins is observed when compared with heating in solution. The helix of the peptide is found to be much less stable thermally than the helices of lysozyme, reinforcing the importance of long-range forces in defining the protein structure. Contact map analysis of the adsorbed proteins shows correlation between the hydrophobicity of the secondary structure and their thermal stability on the surface.

Graphical abstract: Thermal stability limits of proteins in solution and adsorbed on a hydrophobic surface

Back to tab navigation

Supplementary files

Publication details

The article was received on 02 Jan 2012, accepted on 29 Mar 2012 and first published on 30 Mar 2012


Article type: Paper
DOI: 10.1039/C2CP00005A
Citation: Phys. Chem. Chem. Phys., 2012,14, 8013-8022
  •   Request permissions

    Thermal stability limits of proteins in solution and adsorbed on a hydrophobic surface

    Y. Moskovitz and S. Srebnik, Phys. Chem. Chem. Phys., 2012, 14, 8013
    DOI: 10.1039/C2CP00005A

Search articles by author

Spotlight

Advertisements