亲环素A -环孢菌素A复合物II折叠核心的表征：通过包括迁移率来改进折叠核心预测
Characterizing the folding core of the cyclophilin A - cyclosporin A complex II: improving folding core predictions by including mobility
摘要：
确定蛋白质的折叠核心可以提供有关其折叠过程和动力学的信息。用于鉴定构成折叠核心的氨基酸的实验程序包括氢-氘交换和$Φ$ -值分析，并且可能是昂贵和耗时的。因此，需要改进现有的用于在理论上确定蛋白质折叠核心的方法。在这里，我们使用刚性分析的组合方法，同时粗粒度的模拟蛋白质运动，以提高未结合CypA和CypA-CsA复合物的折叠核心预测。我们发现，在CypA和CypA-CsA的折叠核心的最具体的预测来自交叉的静态刚度分析的结果，在第一软件套件中实现，和模拟的倾向，灵活的运动，使用FRODA工具。
英文摘要：
Determining the folding core of a protein yields information about its folding process and dynamics. The experimental procedures for identifying the amino acids which make up the folding core include hydrogen-deuterium exchange and $Φ$-value analysis and can be expensive and time consuming. As such there is a desire to improve upon existing methods for determining protein folding cores theoretically. Here, we use a combined method of rigidity analysis alongside coarse-grained simulations of protein motion in order to improve folding core predictions for unbound CypA and for the CypA-CsA complex. We find that the most specific prediction of folding cores in CypA and CypA-CsA comes from the intersection of the results of static rigidity analysis, implemented in the FIRST software suite, and simulations of the propensity for flexible motion, using the FRODA tool.
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