β-淀粉样蛋白聚集的简化精确可解模型
A simplified exactly solvable model for beta-amyloid aggregation
摘要：
我们提出了一个精确可解的简化统计力学模型β-淀粉样蛋白聚集的热力学，推广了一个研究得很好的模型蛋白质折叠。单体浓度被明确考虑，以及一个非平凡的依赖于单肽链的微观自由度，无论是在α-螺旋折叠的孤立状态，并在纤维状的。该模型的相图进行了研究，并比较了原纤维形成实验的结果，这是定性再现。
英文摘要：
We propose an exactly solvable simplified statistical mechanical model for the thermodynamics of beta-amyloid aggregation, generalizing a well-studied model for protein folding. The monomer concentration is explicitly taken into account as well as a non trivial dependence on the microscopic degrees of freedom of the single peptide chain, both in the alpha-helix folded isolated state and in the fibrillar one. The phase diagram of the model is studied and compared to the outcome of fibril formation experiments which is qualitatively reproduced.
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