Comparative study on the conformational stability of human and murine amyloid β peptide
✍ Scribed by Liang Shen; Hong-Fang Ji
- Book ID
- 119221068
- Publisher
- Elsevier
- Year
- 2011
- Tongue
- English
- Weight
- 462 KB
- Volume
- 972
- Category
- Article
- ISSN
- 2210-271X
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## Abstract **Summary:** The conformational change of the 39–43 residues of the amyloid __β__‐peptide (A__β__) toward a __β__‐sheet enriched state promotes self‐aggregation of the peptide molecules and constitutes the major peptide component of the amyloid plaques in Alzheimer patients. The crucial
Molecular dynamics simulations and simulated annealing in vacuum, model aqueous solution, and simulated membrane were used to analyze the conformational preferences of a segment spanning 20-29 residues of human islet amyloid polypeptide, [referred to as IAPP H (20-29)]. Molecular dynamics simulation