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 c...
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| Veröffentlicht in: | Physical review. E, Statistical, nonlinear, and soft matter physics Statistical, nonlinear, and soft matter physics, 2005-10, Vol.72 (4 Pt 1), p.041912-041912, Article 041912 |
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| container_end_page | 041912 |
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| container_issue | 4 Pt 1 |
| container_start_page | 041912 |
| container_title | Physical review. E, Statistical, nonlinear, and soft matter physics |
| container_volume | 72 |
| creator | Ji, Yong-Yun Li, You-Quan Mao, Jun-Wen Tang, Xiao-Wei |
| description | 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. |
| doi_str_mv | 10.1103/PhysRevE.72.041912 |
| format | Article |
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| identifier | ISSN: 1539-3755 |
| ispartof | Physical review. E, Statistical, nonlinear, and soft matter physics, 2005-10, Vol.72 (4 Pt 1), p.041912-041912, Article 041912 |
| issn | 1539-3755 1550-2376 |
| language | eng |
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| source | MEDLINE; American Physical Society Journals |
| subjects | Amino Acid Sequence Binding Sites Computer Simulation Dimerization Models, Chemical Models, Molecular Molecular Sequence Data Multiprotein Complexes - chemistry Multiprotein Complexes - ultrastructure Prions - analysis Prions - chemistry Protein Binding Protein Conformation Protein Folding Sequence Analysis, Protein |
| title | Model study of prionlike folding behavior in aggregated proteins |
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