Protein structure formation studied by time-resolved infrared spectroscopy (A02)

• Subject Area: Biophysics
• Term: from 2012 to 2023
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 189682160

Understanding the molecular mechanisms of protein folding, misfolding and aggregation is the major objective of this project. We develop time-resolved infrared-spectroscopic techniques to study structure formation on different time scales. Formation of  sheets are analysed on the level of individual amino acids using model peptides and site-specific probes. We design peptide templates with polyglutamine (polyQ) sequences to mimic monomeric structural motifs of a fibril. Backbone ordering and side chain packing will be studied separately in order to shed light onto fibril formation in polyQ diseases. Furthermore, we will extend our IR studies on the intrinsically disordered Parkinson disease protein -synuclein and explore the potential regulatory role of other naturally occurring synuclein variants within the aggregation process. Interaction of aggregates with membranes and membrane damage will be characterized in molecular details.

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 969: Chemical and Biological Principles of Cellular Proteostasis
• Applicant Institution: Universität Konstanz
• Project Head: Professorin Dr. Karin Hauser