Dynamic and Structural Properties of Amyloid Forming and Intrinsically Disordered Polypeptide Chains (A10*)

淀粉样蛋白形成和本质无序多肽链 (A10*) 的动态和结构特性

• 批准号: 276233159
• 金额: --
• 依托单位: Abteilung Proteinbiochemie
• 依托单位国家: 德国
• 项目类别: CRC/Transregios
• 财政年份: 2015
• 资助国家: 德国
• 起止时间: 2014-12-31 至 2018-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/276233159?language=en
• 关键词: Dynamic; Structural; Properties; Amyloid; Forming

The unfolded state of proteins represents the starting point for biologically important processes like folding, assembly, aggregation and amyloid formation. Understanding structural and dynamic properties of unfolded proteins is therefore essential for a detailed understanding of these reactions. In this project we will investigate structure and dynamics of amyloid forming and intrinsically disordered polypeptide chains by a combination of triplet-triplet-energy-transfer and time-resolved fluorescence resonance energy transfer measurements. The results will answer the questions, whether signatures of amyloid formation or the native state, respectively, are already present in the unfolded state.

蛋白质的未折叠状态代表了生物学重要过程如折叠、组装、聚集和淀粉样蛋白形成的起点。因此，了解未折叠蛋白质的结构和动力学特性对于详细了解这些反应至关重要。在这个项目中，我们将通过三重态-三重态能量转移和时间分辨荧光共振能量转移测量的组合来研究淀粉样蛋白形成和内在无序多肽链的结构和动力学。结果将回答问题，无论是淀粉样蛋白形成或天然状态的签名，分别是已经存在于未折叠状态。