(706g) Effect of Surface Hydrophobicity on the Conformational Stability of GB1 Hairpin
AIChE Annual Meeting
Thursday, November 20, 2014 - 2:00pm to 2:15pm
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.