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本文引用的文献

1
Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments.核聚合反应中的次级途径。I. 主要矩的时间演化。
J Chem Phys. 2011 Aug 14;135(6):065105. doi: 10.1063/1.3608916.
2
Nanostructured films from hierarchical self-assembly of amyloidogenic proteins.源自淀粉样蛋白原纤维的分级自组装的纳米结构薄膜。
Nat Nanotechnol. 2010 Mar;5(3):204-7. doi: 10.1038/nnano.2010.26. Epub 2010 Feb 28.
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An analytical solution to the kinetics of breakable filament assembly.可断裂纤维组装动力学的解析解
Science. 2009 Dec 11;326(5959):1533-7. doi: 10.1126/science.1178250.
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Fibril fragmentation enhances amyloid cytotoxicity.原纤维片段化增强淀粉样蛋白的细胞毒性。
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Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature.蛋白质聚集动力学、机制及曲线拟合:文献综述
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Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly.对成核依赖性聚合的系统分析揭示了淀粉样蛋白自组装机制的新见解。
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Mechanisms of protein fibril formation: nucleated polymerization with competing off-pathway aggregation.蛋白质原纤维形成的机制:具有竞争性非途径聚集的成核聚合
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8
Fiber-dependent amyloid formation as catalysis of an existing reaction pathway.纤维依赖性淀粉样蛋白形成作为现有反应途径的催化作用。
Proc Natl Acad Sci U S A. 2007 Jul 24;104(30):12341-6. doi: 10.1073/pnas.0703306104. Epub 2007 Jul 17.
9
The physical basis of how prion conformations determine strain phenotypes.朊病毒构象如何决定毒株表型的物理基础。
Nature. 2006 Aug 3;442(7102):585-9. doi: 10.1038/nature04922. Epub 2006 Jun 28.
10
Protein misfolding, functional amyloid, and human disease.蛋白质错误折叠、功能性淀粉样蛋白与人类疾病
Annu Rev Biochem. 2006;75:333-66. doi: 10.1146/annurev.biochem.75.101304.123901.

核聚合反应中的次级途径。二、用非线性主方程描述的增长过程的自洽解的确定。

Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations.

机构信息

Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.

出版信息

J Chem Phys. 2011 Aug 14;135(6):065106. doi: 10.1063/1.3608917.

DOI:10.1063/1.3608917
PMID:21842955
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5036541/
Abstract

Nucleated polymerisation processes are involved in many growth phenomena in nature, including the formation of cytoskeletal filaments and the assembly of sickle hemoglobin and amyloid fibrils. Closed form rate equations have, however, been challenging to derive for these growth phenomena in cases where secondary nucleation processes are active, a difficulty exemplified by the highly non-linear nature of the equation systems that describe monomer dependent secondary nucleation pathways. We explore here the use of fixed point analysis to provide self-consistent solutions to such growth problems. We present iterative solutions and discuss their convergence behaviour. We establish a range of closed form results for linear growth processes, including the scaling behaviours of the maximum growth rate and of the reaction end-point. We further show that a self-consistent approach applied to the master equation of filamentous growth allows the determination of the evolution of the shape of the length distribution including the mean, the standard deviation, and the mode. Our results highlight the power of fixed-point approaches in finding closed form self-consistent solutions to growth problems characterised by the highly non-linear master equations.

摘要

成核聚合过程涉及自然界中的许多生长现象,包括细胞骨架丝的形成以及镰刀状血红蛋白和淀粉样纤维的组装。然而,在二次成核过程活跃的情况下,对于这些生长现象,很难推导出闭式速率方程,这一难题的一个例子是描述单体依赖性二次成核途径的方程组具有高度非线性的性质。我们在这里探讨使用不动点分析来为这些生长问题提供自洽解。我们提出了迭代解,并讨论了它们的收敛行为。我们为线性生长过程建立了一系列闭式结果,包括最大增长率和反应终点的标度行为。我们进一步表明,将自洽方法应用于丝状生长的主方程可以确定长度分布形状的演化,包括平均值、标准差和模式。我们的结果强调了不动点方法在寻找高度非线性主方程所描述的生长问题的闭式自洽解方面的强大功能。