Local and transient structural features of the intrinsically disordered protein alpha-synuclein (C05*)

本质上无序的蛋白质 α-突触核蛋白 (C05*) 的局部和瞬时结构特征

• 批准号: 283755951
• 金额: --
• 依托单位: Arbeitsgruppe Physikalische und Biophysikalische Chemie
• 依托单位国家: 德国
• 项目类别: Collaborative Research Centres
• 财政年份: 2016
• 资助国家: 德国
• 起止时间: 2015-12-31 至 2018-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/283755951?language=en
• 关键词: Local; transient; structural; features; intrinsically

The classical concept of proteostasis assumes a steady state between folding and misfolding of proteins. This picture gets considerably more complex for intrinsically disordered proteins (IDPs), since they exist in multiple conformational states. The Parkinson protein ¿-synuclein (ASYN) is a model system among the IDPs. A traditional view is that ASYN is disordered in solution and can adopt a variety of stable conformations upon macromolecular interaction. However, findings that ASYN assumes structured features already in solution, suggest an alternative hypothesis for its role in proteostasis that will be investigated in the present project by combining molecular simulation, spectroscopy, and biological in vitro experiments.

蛋白质稳态的经典概念假设蛋白质的折叠和错误折叠之间的稳定状态。对于内在无序蛋白质（IDP）来说，这一情况要复杂得多，因为它们存在于多种构象状态中。帕金森蛋白-突触核蛋白（ASYN）是IDP中的模型系统。 传统的观点认为ASYN在溶液中是无序的，并且可以通过大分子相互作用采取各种稳定的构象。然而，ASYN假设结构化特征已经在解决方案中的研究结果，提出了一个替代假设，其在蛋白质稳定中的作用，将在本项目中结合分子模拟，光谱学和生物体外实验进行研究。