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

蛋白质的未折叠状态代表了折叠、组装、聚集和淀粉样蛋白形成等重要生物学过程的起点。因此，了解未折叠蛋白质的结构和动力学性质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。这些结果将回答以下问题：淀粉样蛋白形成的特征或原生状态是否已经分别存在于未折叠状态中。

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.