Doctoral student in biochemistry (PA2024/1992)

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 Physical Chemistry and Biochemistry and Structural Biology (Department of Chemistry), include experimental and theoretical research on soft and biological matter. Significant work is devoted to protein self-assembly and co-assembly and interactions with other biomolecules.

The current project is focussed on a class of chaperone proteins that through interactions increase the solubility of other proteins (clients) and thus prevent precipitation, often through amyloid fibril formation. The aim is to understand the fundamentals of chaperone self-assembly as well as chaperone-client interactions and co-assembly. The specific aims include determination of size-distributions, partition coefficients, stoichiometries, equilibrium versus kinetic traps, energy barriers, and elucidation of co-assembly structures over a range of length scales.

The PhD student will be part of a collaborative network of students and researchers at the divisions of Biochemistry and Structural Biology (http://www.cmps.lu.se/biostruct/) and Physical Chemistry (http://www.physchem.lu.se) and at Lund University. The PhD student will be admitted in biochemistry.

The project includes experimental studies of chaperone self-assembly and chaperon-client interactions and co-assembly with amyloid forming proteins. The aim is to characterize and understand the relevant protein-protein interactions involved, and the origin of client solubility enhancement at the molecular level. The studies will involve different chaperones and client amyloid proteins. The experimental studies will include the use of several state-of-the art techniques. Relevant experimental methods that are available include optical and NMR spectroscopy, calorimetry, neutron, X-ray and light scattering techniques, fluorescence correlation spectroscopy, surface plasmon resonance and other surface techniques, as well as optical and electron microscopy and microfluidics diffusional measurements. The PhD student will execute planning, methodology development, experimental work and data analysis. The detailed direction of the research studies, including the choice of experimental techniques and approaches will be decided together with the supervisors.

The main duties of doctoral students are to devote themselves to research studies, which includes participating in research projects and third cycle courses. The work duties will also include teaching and other departmental duties (not more than 20%).

• has been awarded a second-cycle qualification, or
• has satisfied the requirements for courses comprising at least 240 credits of which at least 60 credits were awarded in the second cycle, or
• has acquired substantially equivalent knowledge in some other way in Sweden or abroad.

• At least 120 higher education credits must consist of chemistry courses, of which at least 30 higher education credits are graduate work at advanced level within the chosen major or closely related majors. The special authorization may also have been obtained through other equivalent training, which is tested in each individual case.

• Very good oral and written proficiency in English.
• Good knowledge and skills relevant to the thesis project and the work duties. This includes theoretical knowledge in physical chemistry, biochemistry and biophysical chemistry, as well as practical experience of studies of amyloid proteins and chaperones in terms of their self- and co-aggregation.
• Ability to work independently and to design experiments that can address specific research questions.

Selection for third-cycle studies is based on the student’s potential to profit from such studies. The assessment of potential is made primarily on the basis of academic results from the first and second cycle. Special attention is paid to the following:

• Documented experience of scientific experimental studies of self- and co-assembly processes in lipid, peptide and/or protein systems is a great advantage, as well as both hand-on and theoretical knowledge of one or several of the experimental methods mentioned above.

Consideration will also be given to good collaborative skills, drive and independence, and how the applicant, through his or her experience and skills, is deemed to have the abilities necessary for successfully completing the third cycle programme.

Only those admitted to third cycle studies may be appointed to a doctoral studentship. Doctoral studentships are regulated in the Higher Education Ordinance (1993:100), chapter 5, 1-7 §§.

Applications shall be written in English and include a cover letter containing a research statement summarizing previous research accomplishments and the reasons why you are interested in the position and in what way the research project corresponds to your interests and educational background. The application must also contain a CV, degree certificate or equivalent, and other documents you wish to be considered (grade transcripts, contact information for your references, letters of recommendation, etc.).