NR AUHW
AU Ji,Y.Y.; Li,Y.Q.; Mao,J.W.; Tang,X.W.
TI Model study of prionlike folding behavior in aggregated proteins
QU Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics 2005 Oct; 72(4 Pt 1): 041912
PT journal article
AB 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.
MH Amino Acid Sequence; Binding Sites; Computer Simulation; Dimerization; *Models, Chemical; *Models, Molecular; Molecular Sequence Data; Multiprotein Complexes/*chemistry/ultrastructure; Prions/analysis/*chemistry; Protein Binding; Protein Conformation; Protein Folding; Research Support, Non-U.S. Gov't; Sequence Analysis, Protein
AD Department of Physics, Zhejiang University, Hangzhou 310027, People's Republic of China.
SP englisch
PO USA