Lund University, Faculty of Science, Department of Chemistry (Nfak)

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 work will be 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) on the molecular basis for the positive cooperativity of α-synuclein interaction with membranes. The work will focus on the use and methodology development for super-resolution optical microscopy imaging and high-resolution structure determination using cryo-electron microscopy to study protein self- versus co-assembly with a focus on co-aggregates of amyloid proteins and chaperones or lipid membranes.

Work duties

The main duties involved in a post-doctoral posistion is to conduct research. Teaching may also be included, but up to no more than 20% of working hours. The position shall include the opportunity for three weeks of training in higher education teaching and learning.

The work duties includes for example: 

  • Imaging of pure amyloid fibrils and amyloid co-aggregates with chaperones or membranes by cryo-TEM, including freezing of samples on grids and operating the cryo-TEM.
  • Structure determination of amyloid fibril and amyloid co-aggregates with chaperones or membranes using cryo-EM.
  • Imaging of amyloid fibril and amyloid co-aggregates with chaperones or membranes by super-resolution fluorescence microscopy
  • Protein-protein interaction analysis using SPR technology.
  • Protein expression in bacterial cells.
  • Protein purification using ion exchange chromatography and size-exclusion chromatography.
  • Protein labeling with fluorophores.
  • Kinetics and equilibrium studies of protein amyloid formation.

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:

  • A Ph D in Biochemistry, Biophysical Chemistry, Physical Chemistry or equivalent incluidng in the thesis as least one published paper as first author in a journal with a referee system.
  • Documented hands-on experience of cryo-TEM imaging, including freezing of samples on grids using Vitrobot or Leica plunge freezer and operating cryo-TEM models such as Jeol JEM 2200FS with side entry sample loader and Titan Krios.
  • Documented hands-on experience of structure determination of in-vitro and ex-vivo amyloid fibrils of several different proteins using cryo-EM including data acquisition with SerialEM and EPU and data processing using Relion and cryoSpark.
  • Documented hands-on experience of tag-free protein expression and purification from bacterial expression systems using ion exchange chromatography and size-exclusion chromatography.
  • Documented hands-on experience and expertise in of protein amyloid formation and global kinetic analysis to derive the underlying mechanism.
  • Documented hands-on experience and expertise of amyloid formation mechanism studies using super-resolution fluorescence microscopy.

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.
  • Teaching skills.

Additional assessment criteria:

  • Excellent proficiency in English, spoken and written.
  • Additional publications as first author in journals with a referee system.
  • Documented hands-on experience of automated chromatography systems such as FPLC.
  • Documented experience of purification of amyloid fibrils from tissue samples
  • Excellent personal interaction skills.
  • Experience of supervision of master’s or bachelor’s degree students.

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.

Preferred starting date: 1 January 2025.

Instructions on how to apply

Applications shall be written in English and be compiled into a PDF-file containing:

Applications should include a cover letter stating the reasons why you are interested in the position and in what way the employment corresponds to your qualifications. The application should also contain a CV with list of publication, degree certificate or equivalent, and other documents you wish to be considered (grade transcripts, contact information for your references, letters of recommendation, etc.).

Type of employment Temporary position
Contract type Full time
First day of employment 2025-01-01 or as agreed
Number of positions 1
Full-time equivalent 100
City Lund
County Skåne län
Country Sweden
Reference number PA2024/3400
Contact
  • Sara Linse, +46462228246, sara.linse@biochemistry.lu.se
  • Tyra Lundquister, tyra.lundquister@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
  • SEKO: Seko Civil, 046-2229366, sekocivil@seko.lu.se
Published 06.Nov.2024
Last application date 20.Nov.2024 11:59 PM CET

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