Umeå universitet, Medicinska fakulteten

Umeå University is one of Sweden’s largest higher education institutions with over 37,000 students and about 4,700 employees. The University offers a diversity of high-quality education and world-leading research in several fields. Notably, the groundbreaking discovery of the CRISPR-Cas9 gene-editing tool, which was awarded the Nobel Prize in Chemistry, was made here. At Umeå University, everything is close. Our cohesive campuses make it easy to meet, work together and exchange knowledge, which promotes a dynamic and open culture.

The ongoing societal transformation and large green investments in northern Sweden create enormous opportunities and complex challenges. For Umeå University, conducting research about – and in the middle of – a society in transition is key. We also take pride in delivering education to enable regions to expand quickly and sustainably. In fact, the future is made here.

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The Faculty of Medicine, which consists of 13 departments, is responsible for biomedical research and courses in the field of nursing and health care and has an extensive research and graduate education in more than 80 subjects.

Research project

The Department of Medical Biochemistry and Biophysics is looking for a postdoctoral fellow for 2 years for the project; “Mechanisms of hetero-aggregation in neurodegenerative diseases studied by biophysical methods and atomic force microscopy”.

Amyloid formation is a widespread phenomenon due to the generic property of polypeptide chains to self-assemble into cross-β-sheet superstructures. Amyloid formation is manifested in numerous amyloid-related neurodegenerative diseases, including Alzheimer’s and Parkinson’s. Amyloid formation in neurodegenerative disease is often associated with inflammation, which plays role of a common denominator of those diseases. Inflammation triggers the massive production of proinflammatory S100A8/9 proteins that spontaneously forms amyloids and co-aggregates into hetero-amyloids together with Abeta or alpha-synuclein in Alzheimer’s or Parkinson’s disease, respectively. These events initiate the whole pathological amyloid cascade. Recently, the comorbidity of amyloid diseases was shown to be linked to the co-aggregation of different amyloidogenic proteins. Since amyloids formed by individual polypeptides are highly polymorphic, their co-aggregates add up to the complexity and heterogeneity of the amyloid mixture. There is an unmet need to understand the architecture and mechanisms of self-assembly leading to the formation of hetero-aggregates composed of various amyloid polypeptides. The present project aims to study this process by using a wide range of biophysical and biochemical techniques and atomic force microscopy.

Tasks

The applicant will carry out experimental and computational work on the project, plan and design experiments, present your findings in the group and departmental seminars, write manuscripts, help supervising students and actively contribute to a collegial laboratory culture.

Qualifications

To be eligible for the position you should have a PhD, or equivalent, in biophysics, biochemistry, chemistry, or related discipline. Priority should be given to candidates who have completed their doctoral degree no more than three years before the closing date of the application. A candidate who has completed their degree prior to this may be considered if special circumstances exist. 

We are seeking applicants with experience in atomic force and other microscopy, AFM force measurements, spectroscopic methods such as fluorescence, FTIR, circular dichroism and general knowledge of protein chemistry and biochemistry. It is important that you are able to work in a team. Good oral and written communication skills in English are required.

Application

The application should include;

  • Curriculum Vitae (including publication list)
  • Copies of latest degree certificate(s)
  • Names and contact information of at least three reference persons
  • A cover letter describing your goals for this post-doctoral period (max. one A4 page)

The application should be submitted electronically (PDF format), via our e-recruitment system Varbi at the latest on 5th of December 2021.

Terms

The employment is full-time and limited in time to 24 months. Access from February 1st 2022, or by agreement.

Information

For further information please contact Ludmilla Morozova-Roche, Department of Medical Biochemistry and Biophysics, ludmilla.morozova-roche@umu.se.

Type of employment Temporary position
Contract type Full time
First day of employment By agreement
Salary Monthly
Number of positions 1
Full-time equivalent 100%
City Umeå
County Västerbottens län
Country Sweden
Reference number AN 2.2.1-1515-21
Contact
  • Ludmilla Morozova-Roche, +46 90 786528
Union representative
  • SACO, 090-786 53 65
  • SEKO, 090-786 52 96
  • ST, 090-786 54 31
Published 20.Oct.2021
Last application date 05.Dec.2021 11:59 PM CET

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