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Protein structure and function II

  • 15 credits

Do proteins really need chaperones to fold, how do macromolecular motors assemble and operate, and why do proteins sometimes aggregate to cause neurodegenerative disease?

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 behaviour is extended to kinetics and the functional role of high-energy transition states. 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 contains also 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 are expected to be able to:

    • account for the molecular principles behind the self-organization of proteins
    • 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.

    Modules

    Theory 5 ECTS

    Practical laboratory work 10 ECTS

    Teaching format

    Lectures
    Seminars
    Group projects
    Lab

    Assessment

    Theory, written exam

    Lab, written lab reports, written and oral presentations

    Examiner

    Mikael Oliveberg

    E-mail: mikael.oliveberg@dbb.su.se

  • Contact

    Course responsible

    Mikael Oliveberg

    E-mail: mikael.oliveberg@dbb.su.se

    Chemistry Section & Student Affairs Office:

    Office:        Chemical Practice Laboratory M345
    E-mail:       chemistry@su.se

    https://www.kemi.su.se/english/