Effects of the attractive and repulsive parts of hydrophobic interactions on a helices and ß sheets in small peptides are investigated using a simple atomic potential. Typically, a physical spatial range of attraction tends to favor ß sheets, but a helices would be favored if the attractive range were more extended. We also found that desolvation barriers favor ß sheets in collapsed conformations of polyalanine, polyvaline, polyleucine, and three fragments of amyloid peptides tested in this study. Our results provide insight into the multifaceted role of hydrophobicity in secondary structure formation, including the a to ß transitions in certain amyloid peptides.
|Journal||Physical Review E - Statistical, Nonlinear, and Soft Matter Physics|
|Publication status||Published - 25 Oct 2011|