title: Folding and aggregation of designed proteins.
abstract: Protein aggregation is studied by following the simultaneous folding of two designed identical 20-letter amino acid chains within the framework of a lattice model and using Monte Carlo simulations. It is found that protein aggregation is determined by elementary structures (partially folded intermediates) controlled by local contacts among some of the most strongly interacting amino acids and formed at an early stage in the folding process.
authors.affiliation: Dipartimento di Fisica Universita di Milano and Istituto Nazionale di Fisica Nucleare, I-20133 Milan, Italy.
authors.forename: R A
authors.initials: RA
authors.lastname: Broglia
authors.forename: G
authors.initials: G
authors.lastname: Tiana
authors.forename: S
authors.initials: S
authors.lastname: Pasquali
authors.forename: H E
authors.initials: HE
authors.lastname: Roman
authors.forename: E
authors.initials: E
authors.lastname: Vigezzi
mesh_terms: D000595:Amino Acid Sequence; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009010:Monte Carlo Method; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D010455:Peptides; D011506:Proteins