摘要翻译：
淀粉样蛋白前体含有770个氨基酸，其c端99个氨基酸和淀粉样蛋白4042个氨基酸片段同时二聚和聚集。这个问题已经被广泛地讨论过，这里用热力学标度理论来分析结构因子和动力学的变化趋势。特别关注淀粉样蛋白42以外的家族性阿尔茨海默病突变。标度分析与包括膜在内的广泛对接模拟相联系，从而证实了他们的结果并将其扩展到淀粉样前体。
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英文标题：
《Why Abeta42 Is Much More Toxic Than Abeta40》
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作者：
J. C. Phillips
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最新提交年份：
2018
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分类信息：

一级分类：Quantitative Biology        数量生物学
二级分类：Other Quantitative Biology        其他定量生物学
分类描述：Work in quantitative biology that does not fit into the other q-bio classifications
不适合其他q-bio分类的定量生物学工作
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英文摘要：
  Amyloid precursor with 770 amino acids dimerizes and aggregates, as do its c terminal 99 amino acids and amyloid 40,42 amino acids fragments. The titled question has been discussed extensively, and here it is addressed further using thermodynamic scaling theory to analyze mutational trends in structural factors and kinetics. Special attention is given to Family Alzheimer's Disease mutations outside amyloid 42. The scaling analysis is connected to extensive docking simulations which included membranes, thereby confirming their results and extending them to Amyloid precursor.
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PDF链接：
https://arxiv.org/pdf/1810.12404