β淀粉样蛋白和鸡蛋清纤维的催化成核和p53低聚
Catalytic Nucleation of Amyloid Beta and Hen Egg White Fibrils, and p53 Oligomerization
摘要：
标度理论产生可转移的（甚至普遍的）之间的氨基酸序列和三个标题根本不同的蛋白质的聚集函数的代数和几何关系。除了在早期的p53工作中使用的两个亲水性尺度和β链尺度之外，第二个β链热点尺度显示出对于肿瘤抑制因子p53的寡聚化产生非常准确的结果。这些代数和几何关系可以引起拓扑蛋白质-蛋白质聚集的优势，通过在膜催化表面层的相互作用。
英文摘要：
Scaling theory generates transferable (even universal) algebraic and geometrical relations between the amino acid sequences and the aggregation functions of the three titled radically different proteins. In addition to the two hydropathicity scales and beta strand scales used in earlier p53 work, a second beta strand Hot Spot scale is shown to yield very accurate results for oligomerization of p53, the tumor suppressor. These algebraic and geometrical relations could be caused topologically by the dominance of protein-protein aggregation by interactions in a membrane catalytic surface layer.
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