Lunds universitet, Biokemi & Strukturbiologi, 156708 NAT

Lund University was founded in 1666 and is repeatedly ranked among the world’s top universities. The University has around 47 000 students and more than 8 800 staff based in Lund, Helsingborg and Malmö. We are united in our efforts to understand, explain and improve our world and the human condition.

Lund University welcomes applicants with diverse backgrounds and experiences. We regard gender equality and diversity as a strength and an asset.

Subject description

The Center for Molecular Protein Science (CMPS), Department of Chemistry brings together scientists active within the fields of biochemistry, molecular biophysics, structural biology, and physical and theoretical chemistry. The research includes experimental and theoretical studies of biological matter. We address molecular questions in biological systems, and study biological and designed proteins using a combination of classical and advanced techniques including optical and NMR spectroscopy, surface plasmon resonance, light and X-ray scattering, cryo-electron and fluorescence microscopy and X-ray crystallography. The experimental and theoretical methods used often have their origins in physics. Significant work is devoted to protein self-assembly and co-assembly and interactions with other biomolecules. You will join the research group of Sara Linse at CMPS. The research group primarily investigates peptides and proteins implicated in diseases associated with their aggregation and fibril formation. These systems are characterized using both purified and complex samples. The work is focussed on the thermodynamic basis of protein self- versus co-assembly with a focus on structural investigations of co-aggregates of amyloid proteins and chaperones or of proteins with lipid membranes.

DESCRIPTION OF PROJECT

The project is focused i) on a class of chaperones that through interactions increase the solubility of other proteins (clients) and thereby prevent or delay precipitation and amyloid fibrils and ii) the molecular basis of migraine. The work will focus on the use and methodology development for studies of size distributions, structure, kinetics and thermodynamics of protein self- versus co-assembly with a focus on co-aggregates of amyloid proteins and chaperones. Part of the work will focus on development of a migraine diagnostic biosensor and the derivation of binding proteins for relevant GPCR.

Work duties

The primary responsibility of the postdoctoral position is to conduct research. Teaching duties may be included, but will not exceed one fifth of the total working time. The position also includes the opportunity to complete three weeks of of training in higher education teaching and learning.

Qualification requirements

Appointment to a post-doctoral position requires that the applicant has a PhD, or an international degree deemed equivalent to a PhD, within the subject of the position, completed no more than three years before the date of employment decision. Under special circumstances, the doctoral degree can have been completed earlier

Additional requirements:

  • Very good oral and written proficiency in English.

Assessment criteria and other qualifications

This is a career development position primarily focused on research. The position is intended as an initial step in a career, and the assessment of the applicants will primarily be based on their research qualifications and potential as researchers. Particular emphasis will be placed on research skills within the subject.

For appointments to a post-doctoral position, the following shall form the assessment criteria:

  • A good ability to develop and conduct high quality research.
  • Practical experience with, and knowledge of, cryo-electron microscopy (cryo-EM) for structural analysis of protein aggregates and co-aggregates involving different proteins.
  • Practical experience in investigating protein solubility and theoretical understanding of the underlying aggregation phenomena.
  • Practical experience with, and expertise in, protein purification to ultra-high homogeneity, specifically with regard to α-synuclein or tau.
  • Practical experience with, and knowledge of, spectroscopic and isotope-based techniques to characterize and monitor protein fibrillation and the formation of reaction intermediates.
  • Ability to conduct mechanistic analysis of experimental fibril formation data.
  • Experience in designing experiments to evaluate protein aggregation mechanisms.
  • Practical experience in isotopic labeling of proteins.
  • Practical experience with, and understanding of, the role of molecular chaperones in modulating fibril formation.
  • Practical experience in measuring protein size distributions and knowledge of the underlying association models.
  • Teaching skills.

Additional assessment criteria:

  • Documented experience and theoretical foundation in modeling protein pKa shifts upon association.
  • Practical experience with, and knowledge of, the PICUP (Photo-Induced Cross-Linking of Unmodified Proteins) method.

Consideration will also be given to good collaborative skills, drive and independence, and how the applicant’s experience and skills complement and strengthen ongoing research within the department, and how they stand to contribute to its future development.

Terms of employment

This is a full-time, fixed-term employment of a maximum of 2 years. The period of employment is determined in accordance with the agreement “Avtal om tidsbegränsad anställning som postdoktor” (“Agreement on fixed-term employment as a post-doctoral fellow”) between Lund University, SACO-S and OFR/S, dated 1st February 2022.

Instructions on how to apply

Applications shall be written in English and containing:

  • résumé/CV, including a list of publications,
  • a general description of past research and future research interests (no more than three pages),
  • contact information of at least two references,
  • copy of the doctoral degree certificate, and other certificates/grades that you wish to be considered.

 

 

Type of employment Temporary position
Contract type Full time
First day of employment 2025-10-01 or as agreed
Salary Monthly salary
Number of positions 1
Full-time equivalent 100
City Lund
County Skåne län
Country Sweden
Reference number PA2025/2178
Contact
  • Sara Linse, +46462228246, sara.linse@biochemistry.lu.se
  • Jessica Edwinsson, jessica.edwinsson@kilu.lu.se
Union representative
  • OFR/ST:Fackförbundet ST:s kansli, 046-2229362, st@st.lu.se
  • SACO:Saco-s-rådet vid Lunds universitet, kansli@saco-s.lu.se, kansli@saco-s.lu.se
  • SEKO: Seko Civil, 046-2229366, sekocivil@seko.lu.se
Published 27.Jun.2025
Last application date 11.Jul.2025
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