Short Peptide Amyloid Organization: Stabilities and Conformations of the Islet Amyloid Peptide NFGAIL
โ Scribed by Zanuy, David; Ma, Buyong; Nussinov, Ruth
- Book ID
- 118515736
- Publisher
- Biophysical Society
- Year
- 2003
- Tongue
- English
- Weight
- 786 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0006-3495
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๐ SIMILAR VOLUMES
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
## Abstract Plasma amyloidโฮฒ peptide (Aฮฒ) levels have been suggested as a biomarker candidate for detecting incipient AD. Aฮฒ peptides are known to be sensitive to distinct preanalytical sample handling, which calls for standardised preanalytical procedures. We investigated serum and plasma samples