PTM-Psi:一个python包,以促进对蛋白质结构的翻译后修改及其对动态和功能的影响的计算调查
Daniel Mejia-Rodriguez1, Hoshin Kim1, Natalie Sadler2
1Physical Sciences Division, Physical and Computational Sciences Directorate, Pacific Northwest National Laboratory, Richland, Washington, USA.
Protein science : a publication of the Protein Society
|October 30, 2023
概括
本研究介绍了PTM-Psi,这是一个Python工作流程,用于解释后翻译修改 (PTM) 如何影响蛋白质动态和相互作用. 它展示了GAP2蛋白上的S-化如何影响遥远的残留物,揭示了PTM驱动的序列结构功能关系.
科学领域:
- 生物化学 生物化学
- 计算生物学 计算生物学
- 结构生物学 结构生物学
背景情况:
- 翻译后修饰 (PTM) 对于调节蛋白质功能和分子相互作用,特别是氧化还原反应至关重要.
- 解释PTMs对蛋白质动态和功能的影响是具有挑战性的,因为有许多修改可能性和环境影响.
研究的目的:
- 开发一个计算工作流程来解释PTM如何影响蛋白质特性,动态和相互作用.
- 为分析从实验PTM数据中得出的序列结构功能关系提供一个工具.
主要方法:
- 开发了PTM-Psi,这是一个基于Python的工作流程,集成开源软件.
- 利用量子力学用于非标准的氨基酸力场和分子动力学用于自由能量扰动.
- 采用了对接算法来得分绑定复合体,并分析了GAP2蛋白上的S-化.
主要成果:
- 通过使用GAP2蛋白来解释PTM-Psi对蛋白质结构和功能的影响.
- 显示,溶剂暴露的氨酸的S-化通过连接体运动间接影响埋藏的氨酸的催化活性.
- 已识别的受PTM反应的残留物受氧化还原环境变化影响.
结论:
- PTM-Psi工作流有助于解释PTM诱导的蛋白质行为变化.
- 这项工作为自动化涉及PTMs的分子和系统生物学建模奠定了基础.
- 了解PTM对蛋白质动态的影响对于破译复杂的生物过程至关重要.
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