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

• Subject Area: Physical Chemistry of Molecules, Liquids and Interfaces, Biophysical Chemistry ; Statistical Physics, Nonlinear Dynamics, Complex Systems, Soft and Fluid Matter, Biological Physics
• Term: from 2015 to 2019
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 189853844

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.

• DFG Programme: CRC/Transregios
• Subproject of: TRR 102: Polymers under Multiple Constraints: Restricted and Controlled Molecular Order and Mobility
• Applicant Institution: Martin-Luther-Universität Halle-Wittenberg
• Project Head: Professor Dr. Thomas Kiefhaber, since 7/2015