Postdoctoral position(s) in intrinsically disordered proteins and their interactions
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Postdoctoral position(s) in intrinsically disordered proteins and their interactions
The Kragelund laboratory invites applications for 2- and 3-year postdoctoral positions to work on the role of disordered proteins in interactions and the use of stereochemistry for deciphering molecular contacts and dynamics in these complexes. We have recently described that disordered protein complexes exist (Borgia et al., Nature 2018; Bugge et al.,Nat Commun 2025) and that such complexes can be ambidextrous (Newcombe, Due et al. Nature 2024). Additionally, we have contributed to undertanding the role of disorder in transcription factors and how this enables regulatory mechanisms (Delaforge et al. Nucleic Acid Res, 2024; Theisen et al., et al. Nat Commun 2024; Theisen et al., J Am Chem Soc 2021). We are now using these insights to elucidate molecular determinants of remaining disorder in complexes, the role of disorder in transcription factors, as well as bridging between disordered proteins and the origin of Life.
The positions are funded by the Novo Nordisk Foundation Challenge Grant REPIN and the Carlsberg Foundation Semper Ardens Advance Grant.
Position Responsibilities:
The successful candidate will help shape the direction of the research and use in vitro biophysical and biochemical studies as well as biomolecular NMR spectroscopy and small- angle X-ray scattering to decompose the role and determinants of disorder with links to the origin of Life. The candidate will interface with students at all levels as well as staff scientists in the lab and with collaborators in an interdisciplinary environment that will support their career development. Some teaching of undergraduates will be required.
Minimum Education and/or Training:
The successful candidate should have a PhD in structural biology or in protein biophysics/chemistry/biochemistry. The candidate should demonstrate an academic record of excellence, and a strong interest in the growing field of intrinsically disordered proteins. Experience with biomolecular NMR, protein production and biomolecular condensates will be highly valuable to capitalize on the opportunities of the projects.
About the lab:
The successful candidate will join an international collaborative Centre of Research focused on intrinsically disordered proteins, REPIN (https://www1.bio.ku.dk/english/research/bms/sbinlab/repin/), which is part of the Structural Biology and NMR Laboratory (SBiNLab; https://www1.bio.ku.dk/english/research/bms/sbinlab/). SBiNLab is located at the Department of Biology of UCPH, Copenhagen, Denmark and focuses on elucidating the structure, function and dynamics of proteins, with access to state-of-the-art instrumentation and expertise. SBiNLab joins four interdisciplinary and highly collaborative groups with expertise in protein science, NMR, single-molecule techniques and computation. Combined, the laboratory currently includes 50+ persons of different nationalities.
Terms of employment
The position is covered by the Memorandum on Job Structure for Academic Staff.
Terms of appointment and payment accord to the agreement between the Ministry of Finance and The Danish Confederation of Professional Associations on Academics in the State.
Negotiation for salary supplement is possible.
The application, in English, must be submitted electronically by clicking APPLY NOW below.
Please include
The positions are funded by the Novo Nordisk Foundation Challenge Grant REPIN and the Carlsberg Foundation Semper Ardens Advance Grant.
Position Responsibilities:
The successful candidate will help shape the direction of the research and use in vitro biophysical and biochemical studies as well as biomolecular NMR spectroscopy and small- angle X-ray scattering to decompose the role and determinants of disorder with links to the origin of Life. The candidate will interface with students at all levels as well as staff scientists in the lab and with collaborators in an interdisciplinary environment that will support their career development. Some teaching of undergraduates will be required.
Minimum Education and/or Training:
The successful candidate should have a PhD in structural biology or in protein biophysics/chemistry/biochemistry. The candidate should demonstrate an academic record of excellence, and a strong interest in the growing field of intrinsically disordered proteins. Experience with biomolecular NMR, protein production and biomolecular condensates will be highly valuable to capitalize on the opportunities of the projects.
About the lab:
The successful candidate will join an international collaborative Centre of Research focused on intrinsically disordered proteins, REPIN (https://www1.bio.ku.dk/english/research/bms/sbinlab/repin/), which is part of the Structural Biology and NMR Laboratory (SBiNLab; https://www1.bio.ku.dk/english/research/bms/sbinlab/). SBiNLab is located at the Department of Biology of UCPH, Copenhagen, Denmark and focuses on elucidating the structure, function and dynamics of proteins, with access to state-of-the-art instrumentation and expertise. SBiNLab joins four interdisciplinary and highly collaborative groups with expertise in protein science, NMR, single-molecule techniques and computation. Combined, the laboratory currently includes 50+ persons of different nationalities.
Terms of employment
The position is covered by the Memorandum on Job Structure for Academic Staff.
Terms of appointment and payment accord to the agreement between the Ministry of Finance and The Danish Confederation of Professional Associations on Academics in the State.
Negotiation for salary supplement is possible.
The application, in English, must be submitted electronically by clicking APPLY NOW below.
Please include
- Curriculum vitae
- Diplomas (Master and PhD degree or equivalent)
- Complete publication list
- Name and contact details of two references (e.g. PhD supervisor)
- A cover letter in which you relate your competences to the responsibilities of the position and highlight your experiences in working with IDPs