| NKEC14 |
Biochemistry 2, 12 ECTS credits.
/Biokemi 2/
For:
BKM
KeBi
Kem
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Prel. scheduled
hours: 138
Rec. self-study hours: 182
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Area of Education: Science
Subject area: Chemistry
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Advancement level
(G1, G2, A): G2
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Aim:
The objective of the couse is to give comprehensive knowledge in enzyme kinetics, enzyme mechanisms and methodology for characterization of enzymes and to provide basic knowledge in molecular biology and laboratory techniques used in molecular biology.
After studies well learned the student will have proficiency to:
- Calculate kinetic parameters like kcat, KM, Vmax and KI.
- Interprete the meaning of kinetic parameters in terms of enzyme function.
- Recapitulate the reaction mechansim for some enzymes.
- Describe structure and function of nucleic acids.
- Describe and understand the central dogma in molecular biology.
- Decribe the mechanism of various enzyme involved in replication, transcription and translation
- Explore fundamental laboratory techniques and interprete the obtained data in a written report.
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Prerequisites: (valid for students admitted to programmes within which the course is offered)
Approved General chemistry 1 and attended General chemistry 2 Organic chemsitry 1 and Biochemistrry 1
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:
Protein Chemistry, Protein Engineering, Gene Technology
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Organisation:
The theory is mainly presented in lectures. Solving of problems, discussions of theoretical and practical aspects of experiments in the laboratory are performed in lessons. Theoretical and practical aspects of biochemistry are illustrated in the laboratory course. The results of the experimental work should be presented and discussed in written reports.
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Course contents:
Theory: Structure and function of enzymes. Protein folding, enzyme kinetics with different types of inhibitions. Factors causing enzyme catalysis, characterization of the active site, examples of the reation mechansims of certain enzymes and evolution of proteins. Structure of nucleic acids, molecular genetics, replication, transcription, translation, gene control, eukaryotic and prokaryotic genes, gene technology, molecular immunology and molecular evolution.
Laborations: Purification of a protein with ionic change chromatography. Functional analysis of enzymes: Enzyme activity measurement, pH-dependance, chromatogram, kinetic- and spectrophotometric studies. Microbiological work and gene technology experiments
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Course literature:
Berg, Tymoczko & Stryer: Biochemistry, 6th edition. Laboratory manual from the department.
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Examination: |
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Written examination Laboartory work Laboartory work |
8 ECTS 2 ECTS 2 ECTS
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The exercises of the written examination and the test elucidate how well the student perform the the demands of the course.
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Course language is Swedish.
Department offering the course: IFM.
Director of Studies: Stefan Svensson
Examiner: Magdalena Svensson och Lars Göran Mårtensson
Course Syllabus in Swedish
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