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Protein structure and function I

Evolution works by selection of point mutations, but precisely how do these point mutations affect the molecular behavior of the produced proteins? You will learn this during the course!

Botolinumtoxin struktur och kristaller
The botulinum neurotoxins are the most toxic substances known; they are one million times more toxic than the cobra toxin. In spite of their extreme toxicity there has been a rapid expansion of the medical applications for the botulinum neurotoxins. The toxins are studied using variety of methods, including X-ray crystallography and cryo-EM.

Evolution starts by the random and natural generation of point mutations in protein encoding genes. They can be silent and they can be loud and they are a natural consequence of replication in any organism where only favorable mutations are retained in the organism’s progeny. Depending on where these mutations are located in a protein’s three-dimensional structure they may lead to consequences for i.e. its folding, its activity, its intracellular interactions, its longevity in the cell and even a specific phenotype.

The function of a protein is tightly connected to its three-dimensional structure which can be determined using X-ray crystallography. In this course you will learn by doing.

You will learn how to determine a protein’s three-dimensional structure using X-ray crystallography structures from purified protein and subsequently explore how the protein’s property and function respond to point mutations.

The central focus is to understand how the detailed amino-acid interactions determine protein structural stability and binding. In this course you will be introduced to how theory, wet-labs and computing go hand-in-hand to solve real problems in protein chemistry.

In addition, 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 and poster presentations.

  • Course structure

    The course deals with the structure and properties of proteins, with a focus on sequence content and the effect of mutations. During the course you will learn about the following:
    • The ability for reductionist thinking and generalization
    • Quantitative description
    • Formulation and testing of hypotheses according to falsification
    • Proficiency in using laboratory techniques for problem solving
    • Proficiency in computer-based methods and bioinformatics.
    Expected learning outcomes
    After completing the course the student is expected to be able to:
    • Explain the molecular principles behind the structure of proteins 
    • Describe entropy - enthalpy compensation in macromolecular systems and how it controls stability and structural properties
    • explain mutation effects on protein stability and function, as well as the principles of structural evolution
    • Formulate and test hypotheses about the structure, stability and function of proteins, as well as demonstrate proficiency in quantitative description and interpretation of experimental results
    • Independently solve problems through the design of equilibrium experiments.

    Modules

    • Theory, 5 ECTS
    • Laboratory exercises, 2.5 ECTS

    Teaching format

    • Lectures
    • Group projects
    • Seminars
    • Lab work

    Assessment

    Theory - thorugh a written exam

    Laboratory exercises - written and oral reports, mini conference presentation

    Examiner

    Ville Kaila
    ville.kaila@dbb.su.se

  • 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
    Ville Kaila

    Professor

    ville.kaila@dbb.su.se
    Ville Kaila
    Chemistry Section & Student Affairs Office
    Chemistry Section & Student Affairs Office
    chemistry@su.se
    08-16 37 09
    Expen
    • Visiting address

    • Arrheniuslaboratoriet, room M345

    • Svante Arrhenius väg 16 A-D

    • In charge of:

      Bachelor's and Master's education, application, admission, registration, examination

      Here you will get support form:

      Student administrator

      International coordinator

      Student advisor

      Director of studies

    • Office hours

    • Mondays, Tuesdays and Wednesdays 09.00-11.30 and 12.30-15.00

    • Phone hours

    • Mondays and Wednesdays 10.00-11.30 and 12.30-15.00

Selected reading

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