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Protein structure and function II

Do proteins really need chaperones to fold, how do macromolecular motors assemble and operate, and why do proteins sometimes aggregate to cause neurodegenerative disease? These questions are dealt with in this course, where equilibrium behavio is extended to kinetics and the functional role of high-energy transition states.

Information for admitted students Autumn 2023

Congratulations! You have been admitted at Stockholm University and we hope that you will enjoy your studies with us.

In order to ensure that your studies begin as smoothly as possible we have compiled a short checklist for the beginning of the semester.

Follow the instructions on whether you have to reply to your offer or not.


Checklist for admitted students

  1. Activate your university account

    The first step in being able to register and gain access to all the university's IT services.

  2. Register at your department

    Registration can be done in different ways. Read the instructions from your department below.

  3. Read all the information on this page

    Here you will find what you need to know before your course or programme starts.


Your seat may be withdrawn if you do not register according to the instructions provided by your department.

Information from your department

On this page you will shortly find information on registration, learning platform, etc.

Welcome activities

Stockholm University organises a series of welcome activities that stretch over a few weeks at the beginning of each semester. The programme is voluntary (attendance is optional) and includes Arrival Service at the airport and an Orientation Day, see more details about these events below.
Your department may also organise activities for welcoming international students. More information will be provided by your specific department. 

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Stockholm University's main campus is in the Frescati area, north of the city centre. While most of our departments and offices are located here, there are also campus areas in other parts of the city.

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In this course you will learn, hands on, how to structurally characterise protein-folding transition states by protein engineering, structural determination of large complexes by cryo-EM and protein NMR.

The course also contains an introduction to how cells orchestrate and maintains protein function at molecular level and outlines the current view and complexity of protein-aggregation disease.

The key aim is to understand the concept of how amino-acid properties control (i) protein self-assembly and (ii) higher-order processes such as solubility, behaviour in crowded intracellular environments, and protein aggregation.

The basic theme of the course is that theory, wet-labs and computing go hand-in-hand to solve real problems in protein chemistry.

As such, reductionist thinking, application of basic chemical models and data quantification constitute a red thread throughout the teaching, and several common spectroscopic methods and experimental approaches are employed in depth.

Experimental results, progress and student conclusions will be presented/examined both in form of individual seminars, written reports and poster presentations.

  • Course structure

    After the course the student is expected to be able to:

    • Account for the molecular principles behind the self-organization of proteins
    • Describe conformational changes and aggregation
    • Describe the determination of molecular structure and biological mechanism by
      • (i) X-ray crystallography
      • (ii) NMR
      • (iii) cryo-EM
      • (vi) mutation analysis
    • Formulate and test hypotheses about protein interaction and kinetics, as well as demonstrate proficiency in quantitative description, interpretation of experimental results, prediction of mechanism and plausibility estimation.
    • Independently solve problems by designing time-resolved experiments.


    Theory, 10 ECTS

    Practical laboratory work, 5 ECTS

    Teaching format

    Group projects


    Theory - written exam

    Lab - written lab reports, written and oral presentations


    Mikael Oliveberg

  • Schedule

    The schedule will be available no later than one month before the start of the course. We do not recommend print-outs as changes can occur. At the start of the course, your department will advise where you can find your schedule during the course.
  • Course literature

    Note that the course literature can be changed up to two months before the start of the course.

    Required reading material is handed out during the course.

  • Contact

    Course coordinator and examiner
    Chemistry Section & Student Affairs Office