3514.19 - Biochemistry

Course number
A) Admitted to the bachelor programme in biology at the University of the Faroe Islands, and following the normal study progression or B) Students following single courses need to have sufficient background in general and organic chemistry, like: 3512 General and inorganic chemistry; 3513 Organic chemistry.
To provide the students with knowledge of biological molecules (their structures, functions and mechanisms of action) and central metabolic pathways, giving the foundations of molecular life sciences, including the understanding of the biochemistry in organisms.
Biological molecules and their bonds; pH; hydrophilicity and hydrophobicity; the concept of thermodynamics (free energy, enthalpy, entropy); proteins and their structures; lipids and membranes; carbohydrates; nucleic acids and their structures; coenzymes; enzymes; enzyme kinetics and inhibition; glycolysis and gluconeogenesis; ß-oxidation and fatty acid synthesis; citric acid cycle; electron transport chain and oxidative phosphorylation; nitrogen metabolism; DNA replication; transcription; protein synthesis. Laboratory exercises: Enzyme kinetics; polymerase chain reaction. Minor demonstrations.
Learning and teaching approaches
Lectures and problem solving. Laboratory exercises (obligatory) and laboratory report submissions (obligatory).
Learning outcomes
On completion of the course, the successful student should be able to: 1. Describe the chemical basis of life. 2. Describe the chemical and biological properties and the functions of the major groups of biological molecules (both monomeric and polymeric molecules). 3. In simple terms describe the connection between energy and metabolisms on the one hand, and thermodynamics on the other hand, and use thermodynamic equations to support these arguments. 4. Explain the properties (polarity, hydrogen bonds, pH) of water, and why these properties are important for life. 5. Explain in some detail the structures and functions DNA and RNA. 6. Explain the connection between genes and proteins. 7. Explain the structure of DNA. 8. Describe replication of DNA, and explain how this is related to the structure of DNA. 9. Explain and demonstrate how the structure of DNA can be used experimentally to achieve the copying of DNA (PCR). 10. Describe the properties of the most common secondary structures of peptide chains, and how the secondary structures participate in the properties of both structure and functions of the intact proteins. 11. Explain how enzymes work and how amino acids in the catalytic site participate in the most common catalytic mechanisms. 12. Determine by simple mathematical means and graphical means the most basic types of enzyme inhibition, and describe and explain the most basic enzymatic mathematical parameters (KM, Vmax, kcat, etc). 13. Describe some of the central metabolic pathways (glycolysis, gluconeogenesis, the citric acid pathway, oxidative phosphorylation and the electron transport chain, fatty acid oxidation, fatty acid synthesis, nitrogen fixation and assimilation), how they are connected, and how organisms get chemical energy from the catabolic pathways (oxidative phosphorylation). 14. Describe how RNA is made using DNA as template. 15. Describe how mRNA is translated into proteins (keywords: genetic code, ribosomes, rRNA, tRNA, mRNA).
Assessment method
Combination of 1) accepted laboratory reports and 2) graded written examination. 1) The obligatory laboratory reports must be delivered within the specified deadlines. The reports must be accepted (no grading) by the instructor. 2) Four-hour written examination. No auxiliary materials allowed, except for electronic calculator. When the laboratory reports have been accepted, they are also valid in case of re-examination or if following the course once more.
Marking scale
Essential Biochemistry 3. ed., Pratt CW, Cornely K (2014) Wiley, 744 pages. ISBN: 978-1-118-08350-5 (Hardcover); 978-1-118-54962-9 (E-text)
Jónrit Halling