Researcher in Biophysical Chemistry - Hiring in process/Finished, not possible to apply

Description of the workplace
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. We study biological and designed protein systems 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.

You will join the research group of Sara Linse, Biochemistry & Structural Biology in close collaboration with Ulf Olsson, Physical Chemistry. The work will be focussed on protein self- and co-assembly into amyloid fibrils as well as chaperone-amyloid protein co-aggregates using a range of molecular biology, spectroscopic and surface techniques.

Subject description
Biophysical chemistry involves research directed towards molecular questions in biological systems. The experimental and theoretical methods used often have their origins in physics. The biophysical chemistry research within the divisions of Biochemistry and Structural Biology, Biophysical Chemistry as well as Physical Chemistry (Department of Chemistry) includes experimental and theoretical research on biological matter. Significant work is devoted to protein self-assembly and co-assembly and interactions with other biomolecules. The current project focuses on a class of chaperones that through interactions increase the solubility of other proteins and thereby prevent or delay precipitation and amyloid formation.  The work will focus on the structure and function of transient and end-state co-aggregates of chaperones and amyloid proteins.

Work duties
The main duty of a researcher position is to conduct research. The supervision of students at Bachelor and Master level may also be included.

The work will focus on the study of protein self-assembly and chaperone-protein co-assembly reactions with an aim to understand the thermodynamic basis of a class of chaperones that enhance the solubility of other proteins, clients. Studies of chaperone effects on self-assembly processes will also be included with an aim to measure the effect on the rates of underlying in the self-assembly process.

Work duties involves:
Experimental studies of chaperone self-assembly, chaperon-client interactions and co-assembly with amyloid forming proteins. The aim is to characterize and understand the fundamental protein-protein interactions involved, and the origin of client solubility enhancement at the molecular level using fluorescence, circular dichroism and NMR spectroscopy, scattering techniques, surface plasmon resonance technology and calorimetry. The work will include the expression and purification of chaperones and amyloid proteins. The work will include methodology development for a range of biophysical experiments aiming at the determination of size-distributions, partition coefficients, stoichiometries, equilibrium versus kinetic control, energy barriers, and co-assembly structures over a range of length scales.

You will have specific responsibility for protein expression, purification, methodology development for a range of biophysical experiments, execution of such experiments and data analysis. You will be responsible for detailed documentation of all experiments and writing of scientific papers.

Qualification requirements

Applicants must have:

• A PhD or equivalent research qualification within the subject of the position (physical chemistry, biophysical chemistry or biochemistry) with a focus on the molecular factors governing amyloid formation.
• Very good oral and written proficiency in English.
• Excellent knowledge and documented expertise in experimental biophysical studies of protein self-assembly, including fluorescence and circular dichroism spectroscopy and surface plasmon resonance technology.
• Excellent knowledge and documented expertise in global kinetic analysis for the determination of self-assembly mechanisms and rate constants of the underlying steps in the mechanisms.
• Excellent knowledge and documented expertise in protein expression and purification of tag-free protein using ion exchange, hydrophobic interaction and size exclusion chromatography.
• Documented expertise in the development of purification methods including these tools.
• Good analytical skills and programming skills in Python. 
• Ability to work independently and to formulate and tackle research problems.

Assessment criteria and other qualifications
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. A successful applicant will also have been involved as project co-supervisor or mentor of bachelor or master level students.

Consideration will also be given to 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
Permanent full-time position with preferred start date 2025-01-01. A probationary period of 6 months may be applicable. 

Instructions on how to apply
Applications shall be written in English and be compiled into a PDF-file containing a CV with a list of publications as well as a personal letter justifying your interest in the position and how it matches your qualifications. The application should also include a degree certificate or equivalent and any other document to which you would like to draw attention (copies of grade transcripts, details of referees, letters of recommendation, etc.).