Postdoc in Biological Roles of Protein Aggregate Stability, achieve a profound mechanistic understanding of protein and peptide assembly
The research group of Prof. Alexander K. Buell at the department of Biotechnology and Biomedicine (DTU Bioengineering) at Technical University of Denmark is looking to recruit a postdoctoral fellow, to start as soon as possible. Our research group is situated within the section of Protein Chemistry and Enzyme Technology, where world-leading expertise in protein chemistry and structural biology is concentrated. Our laboratory performs cutting-edge experimental research in the field of protein and peptide self-assembly and aggregation. The applied methods include protein engineering as well as various spectroscopy, scattering, biosensing and microfluidics techniques and we work on a range of protein systems the aggregation of which is associated with human disease.
The overall aim of our research is to achieve a profound mechanistic understanding of protein and peptide assembly into ordered (fibrillar, crystalline) and disordered (amorphous, liquid droplet) condensed phases and of the physico-chemical factors and sequence determinants that drive it. To achieve these goals, we also collaborate with structural, computational and medical biologists. The motivation behind our research is to enable rational control of such assembly processes in the context of human disorders, protein biotechnology as well as in the creation of novel types of functional biomaterials.
Research project
In this project, which is funded by the Lundbeck Foundation, the aim is to quantify the thermodynamic stability of various condensed and aggregated states of the proteins alpha-synuclein and TDP-43, as well as variants (mutants, truncated forms and PTMs) thereof. The results of these biophysical experiments will then be compared with the degradability of the aggregates by chaperones and the proteasome. The project will involve collaborations with world-leading researchers in Germany, France and the UK. More detailed information on the project can be obtained on request.
Responsibilities and tasks
The successful candidate will contribute to the establishment of a new experimental methodology with the aim of probing the relationship between protein aggregate stability and degradability. Further tasks will include:
- Assistance in and involvement with other research projects and topics in the group
- Help with the supervision of a PhD student who is also involved in the project
- Taking responsibility for the functioning of research equipment
- Experimental design, data analysis, writing of scientific articles and presentations at conferences and meetings
Qualifications
Candidates must have a PhD degree or equivalent in molecular biology, biophysics or related fields. The successful candidate should:
- Be interested in the quantitative study of biomolecular systems in vitro
- Have documented practical experience with recombinant protein expression and purification, ideally of intrinsically disordered protein systems, as well as their quantitative biophysical characterisation
- Experience with the reconstitution of complex, multi-component biochemical reaction systems in vitro is an advantage
- Feel comfortable in an interdisciplinary research environment of openness and collaboration
- Have a strong track record in the generation, analysis, interpretation and dissemination of scientific results (as demonstrated by peer reviewed publications, oral presentations, teaching and outreach activities)
We offer
DTU is a leading technical university globally recognized for the excellence of its research, education, innovation and scientific advice. We offer a rewarding and challenging job in an international environment. We strive for academic excellence in an environment characterized by collegial respect and academic freedom tempered by responsibility.
Salary and terms of employment
The appointment will be based on the collective agreement with the Danish Confederation of Professional Associations. The allowance will be agreed upon with the relevant union. The period of employment is initially for 2 years.
You can read more about career paths at DTU here.
Further information
Further information may be obtained from Prof. Alexander K. Buell, alebu@dtu.dk. Homepages: Protein Biophysics and Buelllab.
You can read more about the DTU Bioengineering at DTU at www.bioengineering.dtu.dk/english.
If you are applying from abroad, you may find useful information on working in Denmark and at DTU at DTU – Moving to Denmark.
Application procedure
Your complete online application must be submitted no later than 31 May 2022 (Danish time). Apply online at www.career.dtu.dk. Applications must be submitted as one PDF file containing all materials to be given consideration. To apply, please open the link “Apply online”, fill out the online application form, and attach all your materials in English in one PDF file. The file must include:
- Application (cover letter)
- CV
- Academic Diplomas (MSc/PhD – in English)
- List of publications
- Names and contact details of 2-3 referees
Applications received after the deadline will not be considered.
All interested candidates irrespective of age, gender, disability, race, religion or ethnic background are encouraged to apply.
Technology for people
DTU develops technology for people. With our international elite research and study programmes, we are helping to create a better world and to solve the global challenges formulated in the UN’s 17 Sustainable Development Goals. Hans Christian Ørsted founded DTU in 1829 with a clear vision to develop and create value using science and engineering to benefit society. That vision lives on today. DTU has 12,900 students and 6,000 employees. We work in an international atmosphere and have an inclusive, evolving, and informal working environment. DTU has campuses in all parts of Denmark and in Greenland, and we collaborate with the best universities around the world.
Apply for this job
Apply no later than 31 May 2022
Apply for the job at DTU Bioengineering by completing the following form.