title: Model study of prionlike folding behavior in aggregated proteins.
abstract: We investigate the folding behavior of protein sequences by numerically studying all sequences with a maximally compact lattice model through exhaustive enumeration. We get the prionlike behavior of protein folding. Individual proteins remaining stable in the isolated native state may change their conformations when they aggregate. We observe the folding properties as the interfacial interaction strength changes and find that the strength must be strong enough before the propagation of the most stable structures happens.
authors.affiliation: Department of Physics, Zhejiang University, Hangzhou 310027, People's Republic of China.
authors.forename: Yong-Yun
authors.initials: YY
authors.lastname: Ji
authors.forename: You-Quan
authors.initials: YQ
authors.lastname: Li
authors.forename: Jun-Wen
authors.initials: JW
authors.lastname: Mao
authors.forename: Xiao-Wei
authors.initials: XW
authors.lastname: Tang
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D003198:Computer Simulation; D019281:Dimerization; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000648:ultrastructure; D011328:Prions / Q000032:analysis / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D020539:Sequence Analysis, Protein
chemical_list: D046912:Multiprotein Complexes; D011328:Prions