title: Hydrophobic interactions in the formation of secondary structures in small peptides.
abstract: Effects of the attractive and repulsive parts of hydrophobic interactions on α helices and β sheets in small peptides are investigated using a simple atomic potential. Typically, a physical spatial range of attraction tends to favor β sheets, but α helices would be favored if the attractive range were more extended. We also found that desolvation barriers favor β 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 α to β transitions in certain amyloid peptides.
authors.affiliation: Department of Biochemistry and Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada M5S 1A8. diasc@biosimulations.org
authors.forename: Cristiano L
authors.initials: CL
authors.lastname: Dias
authors.forename: Mikko
authors.initials: M
authors.lastname: Karttunen
authors.forename: Hue Sun
authors.initials: HS
authors.lastname: Chan
mesh_terms: D003198:Computer Simulation; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D014867:Water / Q000737:chemistry*
chemical_list: D010455:Peptides; D014867:Water