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Edward Lemke

Synthetic biophysics of protein disorder

Intrinsically disordered proteins (IDPs) are most infamous for their involvement in neurodegenerative diseases, such as Alzheimer’s, Parkinson’s and Huntington’s disease. Almost paradoxically, IDPs are key to many important and precise cellular mechanisms, such as nuclear transport, chromatin packaging, epigenetic regulation and the stress response. IDPs became enriched during evolution and account for 30% of proteins in eukaryotes. The disordered regions make these proteins inherently prone to self-assembling and transforming into amyloids or aggregates, not only in the brain but in the entire organism. Therefore, many age-associated diseases such as cancer, cardiovascular disease, amyloidosis and even diabetes are linked to misregulation of IDPs. In healthy and young cells, this risk is most likely contained by cellular proteostasis mechanisms and outweighed by the intrinsic flexibility and dynamics of IDPs, which are key to orchestrating complex cellular functions through mechanisms that are far from being understood. Our current understanding is that the ability of IDPs to encode multiple functions and complexity apparently outweighs the seeming disadvantages and risks of protein aggregation, 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, constituting what we refer to as the “Dark Proteome”.

Our group uses a multidisciplinary approach centred around superresolved fluorescence technologies, chemical and synthetic biology, and microscope and microfluidic engineering to develop tools and to study the functions of IDPs in eukaryotes, such as their roles in nuclear transport and gene regulation. We aim to understand how function is encoded into the protein sequence of seemingly floppy protein regions and how the cell contains the intrinsic risk of these proteins becoming dysfunctional and molecularly ageing into toxic states, like amyloid fibres.

Research website

Lemke lab website

Positions held

  • Since 2019: Cofounder and Consultant, Araxa (since 2021 Veraxa Biotech GmbH)
  • 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


  • 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

Selected publications by Edward Lemke

Reinkemeier CD and Lemke EA (2021) Dual film-like organelles enable spatial separation of orthogonal eukaryotic translationCell, 184:1–18 Link

Celetti G*, Paci G*, Caria J, VanDelinder V#, Bachand G# and Lemke EA# (2020) The liquid state of FG-nucleoporins mimics permeability barrier properties of nuclear pore complexes. J Cell Biol, 219 (1): e201907157 (*indicates joint contribution, #indicates joint correspondence) Link

Reinkemeier CD, Girona GE and Lemke EA (2019) Designer membraneless organelles enable codon reassignment of selected mRNAs in eukaryotesScience, 363:eaaw2644 Link

Koehler C, Sauter PF, Wawryszyn M, Girona GE, Gupta K, Landry JJM, Fritz MH-Y, Radic K, Hoffmann J-E, Chen ZA, Zou J, Tan PS, Galik B, Junttila S, Stolt-Bergner P, Pruneri G, Gyenesei A, Schultz C, Biskup MB, Besir H, Benes V, Rappsilber J, Jechlinger M, Korbel JO, Berger I, Braese S and Lemke EA (2016) Genetic code expansion for multiprotein complex engineeringNat Methods, 13:997–1000 Link

Milles S, Mercadante D, Aramburu IV, Jensen MR, Banterle N, Koehler C, Tyagi S, Clarke J, Shammas SL, Blackledge M#, Gräter F# and Lemke EA# (2015) Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptorsCell163:734–745 (# indicates joint correspondence) Link