Protein Structure and Function
Syllabus, Master's level, 1KB452
This course has been discontinued.
- Code
- 1KB452
- Education cycle
- Second cycle
- Main field(s) of study and in-depth level
- Chemistry A1F
- Grading system
- Pass with distinction (5), Pass with credit (4), Pass (3), Fail (U)
- Finalised by
- The Faculty Board of Science and Technology, 30 August 2018
- Responsible department
- Department of Chemistry for Life Sciences
Entry requirements
120 credits and knowledge and achievements corresponding to course Spectroscopy, 10 credits. Proficiency in English equivalent to the Swedish upper secondary course English 6.
Learning outcomes
On completion of the course, the student should be able to:
- Analyse the relationship between the structure and function of proteins
- Predict possible functions of a certain protein
- Set up strategies for analysis of the structure and function of proteins
- Give examples of the use of proteins for industrial and other applications
Content
- Protein chemistry: Quantitative amino acid analysis. Peptide sequencing. Chemical modification of proteins.
- Protein synthesis and degradation: Biological and chemical protein synthesis and degradation. Recombinant protein synthesis. Intra-cellular protein degradation. Proteinveckning.
- Protein structure: Determination of the three-dimensional structure of proteins: X-ray diffraction of protein crystals, NMR, microscopy. Computer graphic modelling of proteins. Protein databases and bioinformatics.
- Functional genomics and proteomics: In vitro evolution (with phage display of DNA-binding proteins).
- Protein interactions: Protein-ligand, protein-DNA and protein-protein interactions. Methods for interaction studies. Thermodynamics in interactions.
- Protein function: the importance of different structure levels of proteins for their functional properties. Characterisation of structure-function relationships.
- Examples of protein function and applications:
a. Protein misfolding disorders
b. Receptors and receptor-based drugs
c. Protein-protein interactions, cell signalling
d. Multiprotein complexes, virus.
Instruction
The course is given in the form of lectures and as experimental and theoretical exercises and projects.
Exercises and projects are compulsory and are carried out individually.
Assessment
A comprehensive exam is given at the end of the course, 9 credits. Experimental and theoretical exercises and projects are examined during the course, 6 credits. The final grade is weighted.
If there are special reasons for doing so, an examiner may make an exception from the method of assessment indicated and allow a student to be assessed by another method. An example of special reasons might be a certificate regarding special pedagogical support from the disability coordinator of the university.