Model study of prionlike folding behavior in aggregated proteins.
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.
Ji
Yong-Yun
YY
Department of Physics, Zhejiang University, Hangzhou 310027, People's Republic of China.
Li
You-Quan
YQ
Mao
Jun-Wen
JW
Tang
Xiao-Wei
XW
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
D046912:Multiprotein Complexes; D011328:Prions