On the structural definition of amyloid fibrils and other polypeptide aggregates
✍ Scribed by Fändrich, M. (author)
- Publisher
- Springer
- Year
- 2007
- Tongue
- English
- Weight
- 504 KB
- Volume
- 64
- Category
- Article
- ISSN
- 1420-682X
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📜 SIMILAR VOLUMES
## Abstract Macromolecular crowding is expected to have several significant effects on protein aggregation; the major effects will be those due to excluded volume and increased viscosity. In this report we summarize data demonstrating that macromolecular crowding may lead to a dramatic acceleration
## Abstract Amyloid fibrils are deposited in a number of diseases, including Alzheimer's disease, Type 2 diabetes, and the transmissible spongiform encephalopathies (TSE). These insoluble deposits are formed from normally soluble proteins that assemble to form fibrous aggregates that accumulate in