Edward Lemke

Intrinsically disordered proteins (IDPs) are most famous for their involvement in misfolding neurodegenerative ageing diseases like Alzheimer, Parkinson and Huntington. Almost paradoxically, IDPs are key to many important and precise cellular mechanisms, such as nuclear transport, chromatin packaging, epigenetic regulation and the stress response. Our current understanding is that the ability to encode multiple functions and complexity into these dynamic polymer-like proteins apparently outweighs the seeming disadvantages and risks of misfolding, the chances of which increase with molecular and cellular age. The dynamic nature of IDPs makes their experimental characterisation very difficult, as classical technologies in structural biology like X-ray crystallography and electron microscopy (EM) are limited to largely static systems. Consequently, the disordered part of the proteome remains largely inaccessible to us, constituting what we refer to as the “Dark Proteome”.

Our group uses a multidisciplinary approach centered around superresolved fluorescence technologies, chemical and synthetic biology, microscope and microfluidic engineering to study functional IDPs in eukaryotes, such as in nuclear transport and gene regulation. We aim to understand how function can be encoded into the protein sequence of a seemingly floppy protein and how the cell balances the intrinsic risk of these proteins becoming dysfunctional and ageing to toxic states like the amyloid phenotype.

Research website

Positions held

• Since 2018: Adjunct Director, Institute of Molecular Biology (IMB) & Professor of Synthetic Biophysics, Johannes Gutenberg University (JGU), Mainz
• 2009 - 2020: Group Leader, EMBL, Heidelberg
• 2005 - 2008:  Research Associate (Postdoc), The Scripps Research Institute, La Jolla

Education

• 2005: PhD MPI for Biophysical Chemistry and University of Göttingen
• 2001: Diploma in Chemistry, Technical University of Berlin
• 2001: Master of Science, University of Oklahoma