Effect of Surface Hydrophobicity on the Conformational Stability of GB1 Hairpin

Protein folding in vivo occurs in a crowded cellular environment. The proximity of cellular machinery, macromolecules and even the cell membrane can alter the conformational stability of proteins relative to that in bulk water. Molecular simulation provides a unique opportunity to investigate the factors that effect protein folding near surfaces. We alter the surface hydrophobicity independent of the direct surface-protein attraction between a graphene-like surface and the GB1 hairpin and sample the accessible peptide conformations using replica exchange molecular dynamics. Finally, we discuss the conditions in which water structuring near a surface effects protein adsorption and compare the effect of a hydrophobic surface on Trp-cage miniprotein.