Model study of prionlike folding behavior in aggregated proteins
| Autor: | Jun-Wen Mao, You-Quan Li, Yong-Yun Ji, Xiao-Wei Tang |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Physics Protein Folding Binding Sites Prions Protein Conformation Molecular Sequence Data Phi value analysis Contact order Folding (chemistry) Models Chemical Sequence Analysis Protein Chemical physics Multiprotein Complexes Lattice protein Native state Computer Simulation Protein folding Amino Acid Sequence Downhill folding Dimerization Lattice model (physics) Protein Binding |
| Zdroj: | Physical Review E. 72 |
| ISSN: | 1550-2376 1539-3755 |
| DOI: | 10.1103/physreve.72.041912 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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