标题： 肌红蛋白在朗道-金兹堡-威尔逊方法中的热变性 显示英文标题

标题： Thermal unfolding of myoglobin in the Landau-Ginzburg-Wilson approach

摘要： Landau-Ginzburg-Wilson范式被用于模拟座头鲸肌红蛋白低温晶体学C$\alpha$主链结构。 Glauber协议被用来模拟其对环境温度升高的响应。 发现肌红蛋白通过一系列$\alpha$-螺旋中间体从其天然状态展开，这与变性实验中观察到的折叠和展开模式完全一致。 特别是，识别出一个熔融球状中间体，其具有实验上正确的特性。 构建了一个详细且可实验验证的接触图，以表征展开路径的细节，包括长程相互作用的形成。 结果揭示了蛋白质展开过程如何由其模块化二级结构组分之间的相互作用以及依次熔化所驱动。 显示英文摘要

摘要： The Landau-Ginzburg-Wilson paradigm is applied to model the low-temperature crystallographic C$\alpha$ backbone structure of sperm whale myoglobin. The Glauber protocol is employed to simulate its response to an increase in ambient temperature. The myoglobin is found to unfold from its native state by a succession of $\alpha$-helical intermediates, fully in line with the observed folding and unfolding patterns in denaturation experiments. In particular, a molten globule intermediate is identified with experimentally correct attributes. A detailed, experimentally testable contact map is constructed to characterise the specifics of the unfolding pathway, including the formation of long range interactions. The results reveal how the unfolding process of a protein is driven by the interplay between, and a successive melting of, its modular secondary structure components.