| NKED74 | Protein Chemistry, ECTS-points /PROTEINKEMI/ Advancement level: D | |
| Aim: The course provides comprehensive knowledge in protein chemistry and protein engineering. The relationship between protein structure and biological function is emphasised. The chemical and physical properties of proteins are discussed and how these properties can be utilised to characterise the function of proteins. The laboratory part of the course gives the opportunity to study proteins with modern instruments and analysis methods and to work independently in a project-oriented way. Prerequisites: Courses corresponding to passed NKEA11-13 General Chemistry 1-3, and attended NKEB21 Inorganic Chemistry 2, NKEB22 Organic Chemistry 2, and NKEC52 Biochemistry 2, respectively. Course organization: The theory is presented on lectures and in seminars. Three-dimensional structures of proteins and computer simulations are performed in smaller groups. During the experimental part the students work with genetically mutated human proteins cloned in bacteria. The protein variants are selected after computer graphics studies and are purified and characterised by using modern separation and analysis methodology. The experimental work is guided by laboratory manuals and original scientific articles in order to train independent planning and performance of the experiments. The results of the experimental work is presented and discussed in reports and at seminars. Literature seminars are also held. Course content: Theoretical part: Different structure motifs of proteins. DNA-recognising proteins, multifunctional enzymes, nucleotide binding enzymes, virus structures, recognition of antigens by antibodies, membrane proteins, receptor proteins, prediction, engineering and design of protein structures. Studies of physico-chemical properties of proteins and methodology for studies of these properties: Chemical characteristics of polypeptides, protein engineering, topogenesis, posttranslational modification, evolution and origin of proteins, physical interactions determining the properties of proteins, role of hydrophobic interaction, structure determination by X-ray, NMR and CD, conformation flexibility, protein stability, mechanisms of protein folding, interaction with other proteins, enzyme catalysis. Experimental part: Expression of cloned proteins in bacteria, affinity chromatography, SDS gel electrophoresis, Western blotting, fluorescence measurements, circular dichroism (CD) measurements, amino acid sequence determination, stopped-flow kinetic measurements, computer simulation. Site-directed mutated proteins are purified and characterised. Protein folding studies are performed in a project-oriented way. Course literature: Branden, C. and Tooze, J.: Introduction to protein structure. Creighton, T.E.: Proteins. Structure and molecular properties. Laboratory manual from the department | ||
| LAB 1 | Laboratory course 5 points | |
| TEN 1 | Written examination 2 points | |
| TEN 2 | Written examination 3 points | |