Associate researcher

Ref PAR 2022/1472

The University of Gothenburg tackles society’s challenges with diverse knowledge. 56 000 students and 6 600 employees make the university a large and inspiring place to work and study. Strong research and attractive study programmes attract scientists and students from around the world. With new knowledge and new perspectives, the University contributes to a better future.

Research and graduate education at the department of chemistry and molecular biology comprises a wide scientific field from the atomic and molecular levels all the way through cells to intact organisms. Much of the phenomena studied here impact on our natural environment and living systems. We participate in undergraduate programs in chemistry, molecular biology, medicinal chemistry, biology, marine sciences, and pharmacy.

The group of Björn Burmann uses state of the art NMR-spectroscopy to study large molecular complexes underlying basic cellular functions at the atomic level in combination with other structural biology methods and biophysical characterization. Björn Burmann’s group investigates macromolecular protein machines underlying essential cellular functions, e.g. protein quality control and their effect on misfolding- and aggregation-prone proteins underlying several different diseases, through biophysical and structural biology approaches e.g. high-resolution Nuclear Magnetic Resonance (NMR). Results of previous studies into molecular chaperones and functional mechanism of proteases at the atomic level have been published in top journals (Burmann et al. NSMB 2013, Thoma et al, NSMB 2015, Burmann et al., Nature 2020, Mas et al. Sci. Adv.  2020, Sulskis et al., Sci. Adv. 2021). More details on our research can be found at: (www.wcmtm.gu.se/research-groups/burmann).

Subject area

Structural Biology, Biophysics, and Biochemistry

Subject area description

Structural characterization and biophysical analysis of mechanism of proteases. 

More details on our research can be found at: (www.wcmtm.gu.se/research-groups/burmann).

Duties 

The research project aims at advancing the molecular understanding of the function and regulation of bacterial homo-oligomeric serine proteases by advanced NMR-spectroscopy. Malfunction of these fundamental proteases leads to the accumulation of misfolded proteins and thus provide the foundation for different diseases in humans. Specifically, you will study (1) the molecular mechanisms by which the HtrA2 protease is regulated and activated (2) how it recognizes and subsequently cleaves misfolded protein substrates, and (3) how HtrA2 is regulated by and interacting with auxiliary factors. To achieve this goal, you will use a plethora of techniques ranging from basic biochemistry to advanced structural biology methods and biophysical characterization. Methods in microbiology, molecular biology, bioinformatics and biochemistry will also be used. We are looking for a colleague, that is highly motivated, scientifically independent, and creative, and capable of contributing to a team environment. 

Qualifications 

An advanced degree in a relevant field such as Molecular Biology, Biochemistry, Biophysics, Structural Biology or related fields is expected. Previous work on related protein systems will be considered favorable.

Regulations for the evaluation of qualifications for academic positions are given in Chapter 4, Section 3 - 4 of the Higher Education Ordinance.

The successful candidate should have a strong background in biochemistry, biophysics, and NMR spectroscopy. Previous work related to serine proteases, e.g. expression and purification and/or functional characterization for structural studies, will be considered an advantage. Possessing detailed experience in the following techniques is considered mandatory:

  • Knowledge in recombinant protein expression and purification of relevant proteins, such as human HtrA2.
  • Expert knowledge in solution NMR methods (e.g. assignment, protein dynamics, data analysis)
  • Expert knowledge in sample preparation (isotope labelling, methyl-labelling)
  • Detailed knowledge in additional biophysical and structural biology techniques (ITC, BLI, SEC-MALLS, EM, X-Ray)
  • Documented knowledge in automated data procession and analysis

Furthermore, a genuine interest in structure and dynamics or protein function is required. Co-Authorship in high impact journals such as Nature, Science or Science Advances is considered favorable.

Employment 

Is a fixed term during 6 months fulltime at the Department of Chemistry and Molecular Biology

Contact information for the post 

If you have any questions about the position, please contact
Björn Burmann, Associate Professor, +46(0)31 786 3923 bjorn.marcus.burmann@gu.se

Unions 

Union representatives at the University of Gothenburg can be found here: https://www.gu.se/om-universitetet/jobba-hos-oss/hjalp-for-sokande 

Application 

To apply for a position at the University of Gothenburg, you have to create an account in our recruitment system. Submit your application via the University of Gothenburg’s recruitment portal by clicking the “Apply” button. It is your responsibility to ensure that the application is complete as per the vacancy notice, and that the University receives it by the final application deadline 2022-12-08. 

Please apply online

The application shall include:
Cover letter with an explanation of why you apply for the position

CV including scientific publications
Copy of exam certificate
Two referees (name, telephone no, relation)

Applications must be received by 2022-12-08 

The University works actively to achieve a working environment with equal conditions, and values the qualities that diversity brings to its operations.

Salaries are set individually at the University.

In accordance with the National Archives of Sweden’s regulations, the University must archive application documents for two years after the appointment is filled. If you request that your documents are returned, they will be returned to you once the two years have passed. Otherwise, they will be destroyed.

In connection to this recruitment, we have already decided which recruitment channels we should use. We therefore decline further contact with vendors, recruitment and staffing companies.