dorsal/arxiv
View SchemaThe prion-like folding behavior in aggregated proteins
| Authors | Yong-Yun Ji, You-Quan Li, Jun-Wen Mao, Xiao-Wei Tang |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0506012 |
| URL | https://arxiv.org/abs/q-bio/0506012 |
| DOI | 10.1103/PhysRevE.72.041912 |
| Journal | Physical Review E 72, 041912 (2005), Virtual Journal of Biological Physics Research(October 15, 2005) |
Abstract
We investigate the folding behavior of protein sequences by numerically studying all sequences with maximally compact lattice model through exhaustive enumeration. We get the prion-like 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.
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"abstract": "We investigate the folding behavior of protein sequences by numerically\nstudying all sequences with maximally compact lattice model through exhaustive\nenumeration. We get the prion-like behavior of protein folding. Individual\nproteins remaining stable in the isolated native state may change their\nconformations when they aggregate. We observe the folding properties as the\ninterfacial interaction strength changes, and find that the strength must be\nstrong enough before the propagation of the most stable structures happens.",
"arxiv_id": "q-bio/0506012",
"authors": [
"Yong-Yun Ji",
"You-Quan Li",
"Jun-Wen Mao",
"Xiao-Wei Tang"
],
"categories": [
"q-bio.BM"
],
"doi": "10.1103/PhysRevE.72.041912",
"journal_ref": "Physical Review E 72, 041912 (2005), Virtual Journal of Biological\n Physics Research(October 15, 2005)",
"title": "The prion-like folding behavior in aggregated proteins",
"url": "https://arxiv.org/abs/q-bio/0506012"
},
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