The biochemical genetics of amyloid fibril proteins
β Scribed by Angelo O. Carbonara; Andrea Bottaro
- Publisher
- Springer
- Year
- 1989
- Tongue
- English
- Weight
- 783 KB
- Volume
- 19
- Category
- Article
- ISSN
- 0940-5437
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π SIMILAR VOLUMES
The presence of the antiparallel-&pleated sheet conformation in isolated human amyloid protein fibrils has been confirmed by infrared spectroscopy. In most amyloid samples, this conformation was enhanced by acidic solution conditions. Infrared spectroscopy (Amide I and Amide V absorption bands) and
In a high-salt soluble fraction of the total protein from single seeds of Pinus radiata, up to 45 polypeptides were resolved on SDS-polyacrylamide gels. At least one-fifth of these polypeptides showed variation between seeds. In the 27,000-29,000 dalton region, two polypeptides were inherited as cod
## 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
## 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