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Discrete Molecular Dynamics Study of Alzheimer Amyloid B-protein (AB) Folding

BIOCOMP(2006)

引用 25|浏览10
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摘要
A folding and assembly are believed to be seminal pathogenic events in Alzheimer's disease. We study A (1-42) folding by discrete molecular dynamics using a four-bead protein model with hydrogen bonds and amino acid-specic interactions. Interactions account for hydrophobic/hydrophilic ee ct that mimic the solvent as well as electrostatic ee cts. We study monomer conformations on a wide temperature range. At each temperature, we nd many dier ent monomer conformations, indicating that A (1-42) folding is not unique. At low temperatures, we observe globular conformations with some -helical content while at higher temperatures -strand-rich conformations with no -helical content are present. This temperature-driven conformational change is consistent with experimental ndings by Gursky and Aleshkov. Varying the strength of electrostatics interactions, we show that all monomer conformations become more compact. -strand-rich conformations are characterized by turn regions centered at D23-K28 and G37-G38, and -strands at L17-A21, I31-V36 and V39-A42, which are important in bril formation.
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关键词
discrete molecular dynamics.,protein folding,alzheimer's disease,amyloid -protein,hydrogen bond,amino acid
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