title: Phase diagram of alpha-helical and beta-sheet forming peptides.
abstract: The intrinsic property of proteins to form structural motifs such as alpha helices and beta sheets leads to a complex phase behavior in which proteins can assemble into various types of aggregates including crystals, liquidlike phases of unfolded or natively folded proteins, and amyloid fibrils. Here we use a coarse-grained protein model that enables us to perform Monte Carlo simulations for determining the phase diagram of natively folded alpha-helical and unfolded beta-sheet forming peptides. The simulations reveal the existence of various metastable peptide phases. The liquidlike phases are metastable with respect to the fibrillar phases, and there is a hierarchy of metastability.
authors.affiliation: Centre for Molecular Nanoscience, University of Leeds, Leeds LS2 9JT, United Kingdom.
authors.forename: Stefan
authors.initials: S
authors.lastname: Auer
authors.forename: Dimo
authors.initials: D
authors.lastname: Kashchiev
mesh_terms: D000465:Algorithms; D003198:Computer Simulation; D006860:Hydrogen Bonding; D008956:Models, Chemical; D009010:Monte Carlo Method; D010455:Peptides / Q000737:chemistry*; D044367:Phase Transition; D011336:Probability; D017510:Protein Folding; D055550:Protein Stability; D017433:Protein Structure, Secondary; D012995:Solubility; D012996:Solutions / Q000737:chemistry; D013696:Temperature; D013816:Thermodynamics
chemical_list: D010455:Peptides; D012996:Solutions