The Department of Chemistry Presents, via Webinar: Gabriele S. Kaminski Schierle, Department of Chemical Engineering and Biotechnology, Molecular Neuroscience Group, Cambridge University
How changes in the cellular environment can lead to protein misfolding
Amberley D Stephens, Maria Zacharopoulou, Gabriele S Kaminski Schierle
The protein α-synuclein (aSyn) is an ‘intrinsically disordered protein’ that is highly dynamic in conformation. Transient intramolecular interactions between its charged N and C termini, and between its hydrophobic region and the C terminus, prevent self-association. These interactions inhibit the formation of insoluble inclusions, which are the pathological hallmark of Parkinson’s disease and many other synucleinopathies. In my talk I will discuss how these intramolecular interactions are influenced by the specific environment aSyn is in. In particular, I will discuss how the solvent, charge, calcium, and salt affect the physiological structure of monomeric aSyn, and how they may favour the formation of aggregated structures.
Gabriele Kaminski Schierle is Reader at the University of Cambridge, UK, and Director of the MPhil in Biotechnology. She held a Marie-Curie fellowship during her PhD at Lund University, Sweden (1999), and a Wellcome Trust fellowship to work as a post-doctoral researcher before her appointment as a Lecturer in Cambridge. As head of the Molecular Neuroscience Group, she has built up an internationally recognised research group to investigate the molecular mechanisms causing proteins to form fibrils, and thus pathology in Parkinson’s (PD) and Alzheimer’s Disease (AD). She has set up a state-of-the-art laboratory for the analysis of protein misfolding at a biophysical, biochemical, cellular and small organism level. Kaminski Schierle was awarded a fellowship in the Higher Education Academy for her contribution to teaching and she is co-director of the Cambridge-Infinitus Research Centre, a GBP 10 M venture to study the function of bioactive peptides.
Webinar Link to Be Posted