title: Phase diagram of polypeptide chains.
abstract: We use a coarse grained protein model that enables us to determine the equilibrium phase diagram of natively folded α-helical and unfolded β-sheet forming peptides. The phase diagram shows that there are only two thermodynamically stable peptide phases, the peptide solution and the bulk fibrillar phase. In addition, it reveals the existence of various metastable peptide phases. The liquidlike oligomeric phases are metastable with respect to the fibrillar phases, and there is a hierarchy of metastability. The presented phase diagram provides a solid basis for understanding the assembly of polypeptide chains into the phases formed in their natively folded and unfolded conformations.
authors: Centre for Molecular Nanoscience, School of Chemistry, University of Leeds, LS2 9JT Leeds, United Kingdom. s.auer@leeds.ac.uk
authors: Stefan
authors: S
authors: Auer
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D056004:Molecular Dynamics Simulation; D009010:Monte Carlo Method; D019636:Neurodegenerative Diseases / Q000378:metabolism / Q000473:pathology; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D012996:Solutions / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D000682:Amyloid; D010455:Peptides; D012996:Solutions