Structure of amyloid β fragments in aqueous environments
✍ Scribed by Kazufumi Takano; Shuji Endo; Atsushi Mukaiyama; Hyongi Chon; Hiroyoshi Matsumura; Yuichi Koga; Shigenori Kanaya
- Book ID
- 111310344
- Publisher
- John Wiley and Sons
- Year
- 2006
- Tongue
- English
- Weight
- 318 KB
- Volume
- 273
- Category
- Article
- ISSN
- 1432-1327
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The neurotoxicity of beta-amyloid protein (beta AP) fragments may be a result of their solution conformation, which is very sensitive to solution conditions. In this work we describe NMR and CD studies of the conformation of beta AP(12-28) in lipid (micelle) environments as a function of pH and lipi
## Abstract Amyloid β (Aβ) peptides are one of the classes of amphiphilic molecules that on dissolution in aqueous solvents undergo interesting conformational transitions. These conformational changes are known to be associated with their neuronal toxicity. The mechanism of structural transition in