Skip to main content
Björn Burmann
Photo: Johan Wingborg

Björn Burmann Group

Research group
Active research
Project owner
University of Gothenburg

Short description

Dr. Björn Burmann, Associate Senior Lecturer (Assistant Professor) in Chemistry oriented towards life science.

About Björn Burmann Group

Dr. Björn Burmann, Associate Senior Lecturer (Assistant Professor) in Chemistry oriented towards life science, investigates macromolecular protein machines by high-resolution Nuclear Magnetic Resonance (NMR) underlying essential cellular functions, e.g. protein quality control and DNA-repair processes.

He aims to elucidate their respective function at the atomic level in order to understand their dysfunction underlying several neurodegenerative diseases and cancer-types.

He studies these large molecular protein complexes (~500–800 kDa) by sophisticated NMR-methods, to be able to derive structural and dynamical adaptions of these complexes at the atomic level in solution. These NMR-studies are complemented and combined with additional information from other structural biology and biophysical methods.

These integrated structural biology approaches are used to understand the possible allosteric mechanism of these proteins and their respective complexes underlying their functionality. This knowledge will be used to understand the effect of disease-related mutations and for the subsequent design of either antibiotics or drugs.

International Collaborations

Björn Burmann has extensive international collaborations, which currently include researchers from Columbia University, Harvard University, New York University, University of Leeds, University of Grenoble, University of Lyon, and ETH Zurich, in addition to multiple active local collaborative projects.

Björn Burmann was selected EMBO Young investigator in 2020. He was appointed a Wallenberg Academy Fellow and a Wallenberg Molecular Medicine Fellow in 2017. In addition, he has also been been awarded the Anatole Abragam Price for a Young Investigator in 2017 for his pioneering contributions to the determination of structure and dynamics of chaperone-client complexes at atomic resolution by solution NMR.

Björn Burmann
Photo: Johan Wingborg

Contact Information

Björn Burmann

Department of Chemistry and Molecular Biology
Box 462
405 30 Göteborg

Visiting Address:
Medicinaregatan 9c,
413 90 Gothenburg

Research Summary

The aim of our studies is to understand the structural and dynamical adaptions of molecular machines at the atomic level to be able understand their functionality. We study essential cellular processes whose dysfunction and/or dysregulation are often at the basis of a plethora of different diseases like cancer or neurodegenerative disorders. Subsequently, we plan to use our structural and functional knowledge for the possible future development of new antibiotics and drugs for the associated diseases.

Protein Quality Control

The majority of proteins depend on a well-defined three-dimensional structure to obtain their functionality. In the cellular environment, the process of protein folding is guided by molecular chaperones to avoid misfolding, aggregation, and the generation of toxic species. To this end, living cells contain complex networks of molecular chaperones, which interact with substrate polypeptides by a multitude of different functionalities: transport them towards a target location, help them fold, unfold misfolded species, resolve aggregates, or deliver them towards a proteolysis machinery. Together this system is termed protein quality control (PQR). Owing their dynamical adaptions to be able interact with a wide-range of clients molecualr chaperones are an ideal target to be studies by high-resolution NMR-spectroscopy (Burmann & Hiller, Prog. NMR Spect. 2015). Initial studies on bacterial holdase chaperones revealed a unique interaction mode for the interaction between chaperones and its clients based on avidity and re-orientation of the client on the chaperone surface whereas the client is kept in a folding competent dynamic “fluid-globule” state (Burmann et al., NSMB 2013). Subsequently, a combination of single-molecule force spectroscopy (SMFS) and NMR spectroscopy was employed to characterize how the periplasmic holdase chaperones SurA and Skp shape the folding trajectory of the large β-barrel Omp FhuA from E. coli (Thoma et al., NSMB 2015). The ATP-independent chaperones SurA and Skp prevent unfolded FhuA polypeptide from misfolding by stabilizing a dynamic state, allowing a search for structural intermediates. Ongoing and future work will be dedicated to the detailed study how ATP-dependent unfoldases and proteases recognize and unfold their target proteins. Recent studies have revealed that the Skp chaperone actually exists in a partially unfolded state in the bacterial periplasm, posing interesting possibilities for its function (Mas, Burmann, et al., Sci. Adv. 2020). In parallel we have started working on the main protease in the periplasm DegP, revealing its details of activation using a sophisticated temperature activation mechanism used to alter its oligomeric state (Šulskis, Thoma, Burmann, bioRxiv 2020). Especially, how these molecular machines are able to dissolve protein fibrils and large aggregates, which are often found in Neurodegenerative diseases, will be studied at the atomic level. In fact, our latest studies revealed an important involvement of chaperones even in the physiological function of Parkinson’s related α-synuclein (Burmann et al., Nature 2020; Aspholm, Matečko-Burmann, Burmann, Life 2020).

Transcription Coupled Repair

Bacterial transcription, the production of an RNA transcript from a DNA template, is performed by the RNA polymerase (RNAP). Previous work on a class of transcription factors making RNAP pause-resistant revealed the existence of a direct linkage between transcription and translation machinery, or the RNAP and the ribosome (Burmann et al., Science 2010; Burmann et al., Cell 2013). This work showed the direct connection between different essential machineries in the cell.

In addition RNAP is also directly involved in cell maintenance functions: RNAP functions as a global sensor of DNA-damages subsequently recruiting the DNA-repair machinery, a process termed transcription-coupled repair (TCR) (reviewed in Belogurov & Artsimovitch Annu. Rev. Microbiol. 2015). Ongoing and future work will be dedicated to the detailed study how the repair proteins are recruited to the DNA damage site and how they either disassemble the RNAP or restart it after successful DNA-repair. These studies might open new leads for the design of new antibiotics targeting new important sites on RNAP or other components of the TCR-machinery.

We have recently determined the structure of an important carboxy-terminal domain of the helicase UvrD involved in TCR revealing its role as a binding hub (Kawale & Burmann, Commun. Biol. 2020). Currently, we are focusing on different domains of UvrD to elucidate its functional details.

Integrated Structural Biology Approaches

To study our systems of interest we make mainly use advanced high-resolution NMR-spectroscopy. We have direct access to the Swedish NMR Centre on-site here in Gothenburg, enabling our challenging studies of large protein complexes. In this regard we also plan to further develop and optimize the NMR-methodology for studying these large and complex systems. In order to study the whole functionality of the systems, we employ a comprehensive combination of structural biology techniques besides NMR-spectroscopy, including X-ray crystallography and electron microscopy at state-of-the-art level to obtain atomic resolution representations of the architecture of large protein assemblies. Further we combine our studies with extensively biophysical characterizations to study interactions and structural adaptions.

Novel Approaches for studies in the biological context

To further complement our studies, we are developing novel tools to study these proteins and their complexes within their native environment, the cell or the cellular membrane, respectively. In order to achieve this goal, we have set-up facilities for in-cell NMR spectroscopy in living mammalian cells and are optimizing our experimental approaches (e.g. Burmann et al., Nature 2020, Matečko-Burmann & Burmann, Meth. Mol. Biol. 2020). In parallel, we are also exploiting the usage of bacterial outer membrane vesicles (OMVs) as surrogates for studying integral membrane proteins in their native environment. Our pioneering work on bacterial OMVs revealed, that they are an excellent tool for studying bacterial envelope proteins in their cellular environment (Thoma & Burmann, Biochemistry 2020; Thoma & Burmann, Bio-protocol 2020).

Grants and Awards


  • 2020 Vetenskapsrådet Consolidator Grant
  • 2020 Vetenskapsrådet Research Grantgratefully declined
  • 2019 Cancerfonden Project Grant
  • 2017 Wallenberg Academy Fellowship of the Knut and Alice Wallenberg Foundation, Sweden
  • 2017 Vetenskapsrådet Young Investigator Grant
  • 2013 Ambizione Fellowship of Swiss National Science Foundation
  • 2011 PostDoc stipend of the Novartis Jubilee Foundation


  • 2020 EMBO Young Investigator
  • 2017 Anatole Abragam Prize for a Young Investigator at the ISMAR 2017, Québec City, Canada
  • 2014 MRC Young Scientist Award at the EUROMAR 2014, Zurich, Switzerland

Key Publications

Full list of publications on PubMed

Selected Publications

Burmann B.M., Gerez J.A., Matečko-Burmann I., Campioni S., Kumari P., Ghosh D., Mazur A., Aspholm E.E., Šulskis D., Wawrzyniuk M., Bock T., Schmidt A., Rüdiger S.G.D., Riek R., Hiller S.
Regulation of α-synuclein by chaperones in mammalian cells.
Nature, 577, 127–132 (2020)
F1000 evaluation (Exceptional)

Morgado L., Burmann B.M., Sharpe T., Mazur A. & Hiller S.
The dynamic dimer structure of the chaperone Trigger Factor.
Nature Communications. 1992 (2017)
Link | Press Release, University of Basel

Stanger F.V., Burmann B.M, Harms, A, Aragao H., Mazur A., Sharpe T., Dehio C., Hiller S., Schirmer T.
Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification.
Proc. Natl. Acad. Sci. USA, 113, E529–537 (2016).
F1000 evaluation (Good)

Thoma J.*, Burmann B.M.*, Hiller S., Müller D.J.
Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer membrane proteins.
Nat. Struct. Mol. Biol., 22, 795–802 (2015).
* authors contributed equally
Press Release University of Basel

Burmann B.M., Wang C., Hiller S.
Conformation and dynamics of membrane-protein-transport-chaperone complexes OmpX–Skp and tOmpA–Skp.
Nat. Struct. Mol. Biol., 20, 1265–1272 (2013).
F1000 evaluation (Very Good)
Press Release University of Basel

Burmann B.M., Knauer S.H., Sevostoyanova A., Schweimer K., Mooney R.A., Landick R., Artsimovitsch I., Rösch P.
An α-helix to β-barrel domain switch transforms the transcription factor RfaH into a translation factor.
Cell, 150, 291–303 (2012).
F1000 evaluation (Exceptional)
Cell Preview by V. Svetlov & E. Nudler (New York University)

Burmann B.M., Schweimer K., Luo X., Wahl M.C., Stitt B.L., Gottesman M.E., Rösch P. A NusE:NusG
Complex links transcription and translation.
Science, 328, 501–504 (2010).
F1000 evaluation (Good)
Science Perspective by J.W. Roberts (Cornell University)

Group Members

Laura Troussicot, Post-Doctoral Fellow
(shared with Mikael Molin, CMB)

  • PhD in Biophysical and Chemical Analysis, University of Lyon, France
  • M.Sc. in Analytic Chemistry, University of Orleans, France
  • B.S. in in Applied Chemistry, University of Orleans, France

Ashish Kawale, Post-Doctoral Fellow

  • PhD in Biomolecular NMR Spectroscopy, Technical University Munich, Germany
  • M.Sc. in Biotechnology, IIT Roorkee, India
  • B.Sc. in Biotechnology, Mumbai University, India

Lisa Metzger, PhD, Post-Doctoral Fellow

  • PostDoc in Infection Biology, EPFL Lausanne, Switzerland
  • Ph.D. in Microbiology, ETH Zurich, Switzerland
  • M.Sc. in Molecular Biology, Biozentrum Basel, Switzerland
  • B.S. in Biology, University of Basel, Switzerland

Johannes Thoma, PhD, Post-Doctoral Fellow

  • PostDoc in Biophysics, ETH Zurich, Switzerland
  • Ph.D. in Biophysics, ETH Zurich, Switzerland
  • M.Sc. in Nanosciences, University of Basel, Switzerland
  • B.S. in Nanosciences, University of Basel, Switzerland

Darius Šulskis, PhD student

  • M.Sc. in Biochemistry, Vilnius University, Lithuania
  • B.S. in Biochemistry, Vilnius University, Lithuania

Emelie Aspholm, PhD student

  • M.Sc. in Molecular Biology, Gothenburg University, Sweden
  • B.S. in Molecular Biology, University of Gothenburg, Sweden

Damasus Okeke, PhD student

  • M.Sc. in Biological Chemistry, University of Stavanger, Norway
  • B.Sc. in Biochemistry, University of Nigeria, Nsukka, Nigeria

Ylber Sallova, PhD student

  • M.Sc. in Protein Science, University of Linköping, Sweden
  • B.Sc. in Chemical Biology, University of Linköping, Sweden

Jens Lidman, PhD student

  • M.Sc. in Protein Science, University of Linköping, Sweden
  • B.Sc. in Chemical Biology, University of Linköping, Sweden