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.
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.
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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.
Modules
Theory, 10 ECTS
Practical laboratory work, 5 ECTS
Teaching format
Lectures
Seminars
Group projects
LabAssessment
Theory - written exam
Lab - written lab reports, written and oral presentations
Examiner
Mikael Oliveberg
mikael.oliveberg@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.
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Contact
Course coordinator and examinerMikael OlivebergProfessor
Chemistry Section & Student Affairs Office- Visiting address
Arrhenius laboratory, room M345
Svante Arrhenius väg 16 A-D
- Here you will find:
Student administrator
International coordinator
Study advisor
Director of studies
- Office hours
Monday, Tuesday and Wednesday 09.00-11.30 and 12.30-15.00
- Phone hours
Wednesday 10.00-11.30 and 12.30-15.00
