| NKEC52 | Biochemistry 2, 15 ECTS credits. /Biokemi 2/ |
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Prel. scheduled
hours: 138 |
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Area of Education: Science Subject area: Chemistry |
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| Advancement level
(A-D): C
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| Aim: The course provides comprehensive knowledge in the following areas in biochemistry: Structure and function of proteins, enzymology, bioenergetics, metabolism, structure and function of nucleic acids, molecular genetics. The laboratory course will give training in basic laboratory techniques and illustrate various theoretical aspects. |
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| Prerequisites: (valid for students admitted to programmes within which the course is offered) Approved General Chemistry 1-3, attended NKEB21 Inorganic Chemistry 2, NKEB22 Organic Chemistry 2 and attended courses in biology, 40p corresponding Biology 1 and 2. Note: Admission requirements for non-programme students usually also include admission requirements for the programme and threshhold requirements for progression within the programme, or corresponding. |
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| Supplementary courses: NKED74 Protein Chemistry, NKEC61 Gene Technology |
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| Organisation: The theory is mainly presented on lectures. Solving of problems, discussions of theoretical and practical aspects of experiments in the laboratory course, studies of molecular models, computer simulations of protein purification are performed in smaller groups. Theoretical and practical aspects of biochemistry are illustrated in the laboratory course. The results of the experimental work should be presented and discussed in reports and at seminars. |
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| Course contents: Theoretical part: Structure and function of biomolecules. The cell. Protein purification. Primary-, secondary-, tertiary- and quartenary structure. Protein folding, enzyme kinetics with different forms of inhibition, two-substrate kinetics. Enzyme catalysis, characterisation of enzyme mechanisms, examples of specific mechanisms. Bioenergetics, glycolysis, citric acid cycle, oxidative phosphorylation, photosynthesis, gluconeogenesis, lipid metabolism, amino acid metabolism, control mechanisms. Structure of nucleic acids, molecular genetics, replication, transcription, translation, gene control, eukaryotic and prokaryotic genes, gene technology, molecular immunology and molecular evolution. Experimental part: Protein purification by affinity chromatography. Purity and function analyses of enzymes: Isoelectric focusing, assay of enzyme activity, chromatogram, atomic absorption analysis, preparation of apoenzyme, role of cofactors, kinetic and spectrophotometric studies. Two-substrate kinetics. Microbiological work and gene technology experiments |
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| Course literature: Berg, Tymoczko & Stryer: Biochemistry, 5th Ed. Laboratory manual from the department |
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| Examination: | |||
| Written examination I (metabolism) Written examination II (general biochemistry and molecular genetics) Laboratory course |
2 p 3 p 5 p |
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Course language is Swedish. Department offering the course: IFM. Director of Studies: Stefan Svensson Examiner: Uno Carlsson Course Syllabus in Swedish |
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