Non-native beta-sheet formation: insights into protein amyloidosis
| dc.creator | Guo, Chinlin | |
| dc.creator | Levine, Herbert | |
| dc.creator | Kessler, David A. | |
| dc.date | 2002-03-08 | |
| dc.date.accessioned | 2026-07-07T02:44:39Z | |
| dc.date.available | 2026-07-07T02:44:39Z | |
| dc.description | Protein amyloidosis is a cytopathological process characterized by the formation of highly beta-sheet-rich fibrils. How this process occurs and how to prevent/treat the associated diseases are not completely understood. Here, we carry out a theoretical investigation of sequence-independent beta-sheet formation, based on recent findings regarding the cooperativity of hydrogen-bond network formation. Our results strongly suggest that in vivo beta-sheet aggregation is induced by inter-sheet stacking dynamics. This leads to a prediction for the minimal length of susceptible polymer needed to form such an aggregate. Remarkably, the prediction corresponds quite well with the critical lengths detected in poly-glutamine-related diseases. Our work therefore provides a theoretical framework capable of understanding the underlying mechanism and shedding light on therapy strategies of protein amyloidosis. | |
| dc.identifier | https://arxiv.org/abs/cond-mat/0203200 | |
| dc.identifier | http://arxiv.org/abs/cond-mat/0203200 | |
| dc.identifier.uri | http://salesiana.dossiersoluciones.com/handle/123456789/19015 | |
| dc.subject | Soft Condensed Matter | |
| dc.subject | Statistical Mechanics | |
| dc.subject | Quantitative Biology | |
| dc.title | Non-native beta-sheet formation: insights into protein amyloidosis | |
| dc.type | text |