FaF:FDGBC_FAF Biochemistry - Course Information
FDGBC_FAF Biochemistry
Faculty of PharmacyAutumn 2024
- Extent and Intensity
- 1/1/0. 25 credit(s). Type of Completion: zk (examination).
- Teacher(s)
- Mgr. Marie Brázdová, Ph.D. (lecturer)
- Guaranteed by
- Mgr. Marie Brázdová, Ph.D.
Faculty of Pharmacy - Prerequisites
- FAKULTA(FaF)
The subject is realized through consultations and self-study, assumes the mastering of the study literature and the understanding of the context. - Course Enrolment Limitations
- The course is only offered to the students of the study fields the course is directly associated with.
- fields of study / plans the course is directly associated with
- Pharmacognosy (programme FaF, D-Fg) (2)
- Course objectives
- Biochemistry is aimed at deepening the knowledge of biochemistry obtained in the undergraduate study. It focuses on detailed information on selected chemical processes in living organisms relevant to the study of DSP Pharmacognosy. Special emphasis is placed on modern information and links between biochemistry and molecular biology.
- Learning outcomes
- Deepening basic knowledge of biochemistry forming the basis for related subjects. After completing the course, the student will be able to: - use the information obtained to understand the molecular basis of the effect of many drugs Advanced biochemical methods Knowledge of metabolic processes Cellular signalling pathways
- Syllabus
- Syllabus Biochemistry
1) Biochemistry: Biochemistry of deepening basic knowledge
1.1) Scope of biochemistry: central principles, cellular and chemical foundations (functional groups, reactions), physical foundations
1.2) Living cells (structure of eukaryotic cell)
1.3) Water: the medium of life (interactions, pH, pKa, buffers, blood, liver and urine buffering systems, osmosis, dialysis)
1.4) Energy (free energy, ATP)
2) Structure and function of proteins
2.1) Amino acids (structure, pKa, pI, properties, covalent modifications)
2.2) Peptides (peptide bound, disulfide bridge, glutathione, insulin, antibiotics, neurotransmiters)
2.3) Protein structure (secondary, tertiary, conformation, structure and function)
2.4) Structure and function of hemoglobin and myoglobin
3) Enzymes
3.1) Properties of Enzymes (cofactors, coenzymes, vitamins)
3.2) Classification of Enzymes (examples of each class)
3.3) Catalysis (enzyme reaction, active site, specificity) and Enzyme regulation
3.4) Kinetics of enzyme reactions
4) Membrane transport
4.1) Biomembranes - composition and function
4.2) Membrane transports
5) Carbohydrates and metabolism of carbohydrate
5.1) Monosaccharides, Disaccharides, Oligosaccharides
5.2) Polysaccharides (structure and function)
5.3) Metabolism, homeostasis, catabolism, anabolism, nutrient pool, energy metabolism
5.4) Glycolysis and Glyconeogenesis
5.5) Glycogen metabolism
6) Metabolism of Proteins and Amino Acid Nitrogen
6.1) Overview of metabolism of proteins,
6.2) Elimination of alfa-amino nitrogen
6.3) Detoxification of Ammonia
6.4) Catabolism of Amino Acids (Ala, Arg, Ser, Gly, Thr, Asp, Glu, His, Phe, Tyr, Cys)
7) Aerobic metabolism
6.1) Tricarboxy Acid Cycle (Citric Acid Cycle (overview, fuels, mitochondrion, enzymes and coenzymes, 8 steps of CC, regulation of pyruvate dehydrogenase, control of CC, biosynthesis aspects of CC)
6.2) Respiratory chain (redox potential, sequence of electron carriers)
6.3) Oxidative phosphorylation (enzymes, prosthetic groups, localization in mitochondria, mechanism ATP synthesis)
6.4) Oxidative stress (reactive oxygen species, their formation, antioxidant enzymes systems, antioxidant molecules)
7) Lipids
7.1) Lipids classes (definition, biological) and metabolism
7.2) Synthesis and degradation of Fatty acids
7.3) Lipid synthesis. Peroxidation and Eicosanoids.
7.4 Biotransformation
8) Nucleic acids and their metabolism
8.1) Structure of components, role of nucleotides, biosynthesis (replication, transcription and proteosynthesis
8.2) Nucleic acids metabolism (biosynthesis and degradation of purine and pyrimidine nucleotides)
9) Integration of metabolism and cell signaling
- Syllabus Biochemistry
- Literature
- required literature
- MURRAY,R.K., GRANNER,D.K.,RODWELL,V.W. Harper´s Illustrated Biochemistry. Appleton & Lange, 2006. ISBN 07-147885-X. info
- Robert K. Murray, Daryl K. Granner, Peter A. Mayes, Victor W. Ro. Harperova biochemie. ČR, 2002. ISBN 80-7319-013-3. info
- CHAMPE,P.C.,HARVEY,R.A. Lippincott´s Illustrated Reviews: Biochemistry. Lippincott Wiliams & Wilkins, 1994. ISBN 0-397-51091-8. info
- not specified
- MURRAY,R.K., GRANNER,D.K.,MAYES,P.A.,RODWELL,V.W. Harperova biochemie (český překlad). Nakladatelství a vydavatelství H & H, 1993. ISBN 80-85787-38-5. info
- APPS,D.K.,COHEN,B.B.,STEEL,C.M. Biochemistry (A concise text for medical students). Bailliére Tindall, 1992. ISBN 70-20-1444-3. info
- Teaching methods
- Methods of working with text (textbook, book) Discussion,self-study of lectures, textbooks, exercise books
- Assessment methods
- Written and oral exam. The written part, which consists of a test with 40 questions, 150 points. To successfully complete the course, it is necessary to pass the test at 60%.
- Language of instruction
- Czech
- Further comments (probably available only in Czech)
- The course can also be completed outside the examination period.
The course is taught each semester. - Teacher's information
- Requirements for the student
Successful completion of the subject by written and oral examination. The mark is based mainly on the part of the test. To pass the course, you must pass the test at 60%.
- Enrolment Statistics (recent)
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