A collection of programs is presented to analyze the thermodynamics of folding of linear repeat proteins using a 1D Ising model to determine intrinsic folding and interfacial coupling free energies. Expressions for folding transitions are generated for a series of constructs with different repeat numbers and are globally fitted to transitions for these constructs. These programs are designed to analyze Ising parameters for capped homopolymeric consensus repeat constructs as well as heteropolymeric constructs that contain point substitutions, providing a rigorous framework for analysis of the effects of mutation on intrinsic and directional (i.e., N‐ vs. C‐terminal) interfacial coupling free‐energies. A bootstrap analysis is provided to estimate parameter uncertainty as well as correlations among fitted parameters. Rigorous statistical analysis is essential for interpreting fits using the complex models required for Ising analysis of repeat proteins, especially heteropolymeric repeat proteins. Programs described here are available at https://github.com/barricklab-at-jhu/Ising_programs.

中文翻译：

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具有点替换的线性重复蛋白的一维 Ising 分析程序集

提供了一系列程序来使用 1D Ising 模型分析线性重复蛋白质折叠的热力学，以确定内在折叠和界面耦合自由能。为一系列具有不同重复数的构造生成折叠转换表达式，并全局拟合这些构造的转换。这些程序旨在分析加帽的同聚重复构建体以及包含点取代的异聚体构建体的 Ising 参数，为分析突变对内在和方向（即 N 端与 C 端）的影响提供了严格的框架界面耦合自由能。提供引导分析以估计参数不确定性以及拟合参数之间的相关性。严格的统计分析对于使用重复蛋白质（尤其是异聚重复蛋白质）的 Ising 分析所需的复杂模型来解释拟合至关重要。此处描述的程序可从 https://github.com/barricklab-at-jhu/Ising_programs 获得。