Course code:
409H1		 Course name:
Biochemistry

Academic year:

2019/2020.

Attendance requirements:

200A1 + 200E1

ECTS:

6

Study level:

basic academic studies

Study program:

Chemistry: 4. year, winter semester, compulsory course

Teachers:

Natalija Đ. Polović, Ph.D.
full professor, Faculty of Chemistry, Studentski trg 12-16, Beograd

Milica M. Popović, Ph.D.
associate professor, Faculty of Chemistry, Studentski trg 12-16, Beograd

Assistants:

Jelica R. Milošević, Ph.D.
assistant professor, Faculty of Chemistry, Studentski trg 12-16, Beograd

Nemanja D. Mijin

Lidija Đ. Filipović
research assistant, Innovation center, Studentski trg 12-16, Beograd

Hours of instruction:

Weekly: three hours of lectures + three hours of labwork (3+0+3)

Goals:

The goal of this course is to introduce students to the molecular foundations of living organisms, to the uniqueness and diversity of biochemical processes, to help them understand the importance of chemistry for living organisms and to help them master the basic experimental skills needed for working in biochemical laboratories.

Outcome:

Understanding the essential concepts of biochemistry at the basic level. Students should be familiar with the rules for working in a biochemical laboratory and with the basic experimental skills used in it.

Teaching methods:

Lectures, experimental exercises.

Extracurricular activities:

—

Coursebooks:
  • Lubert Stryer: Biochemistry
  • Vesna Niketić: Uputstva za vežbe iz biohemije
  • Vesna Niketić: Principi strukture i aktivnosti proteina
  • J. Koolman, K.H. Roehm: Color Atlas of Biochemistry, 2005.
  • D. L. Nelson, M. M. Cox, Lehninger: Principles of Biochemistry, 2000.

Additional material:

—

  Course activities and grading method

Lectures:

3 points (3 hours a week)

Syllabus:

  1. Introduction: What is biochemistry all about (molecular logic of life).
  2. The cell structure of prokaryotes and eukaryotes.
  3. Proteins: three-dimensional structure (conformation; conformational stability; conformational transition: protein folding/unfolding).
  4. Comparative description of protein structure and activity (protein-ligand interaction).
  5. Hemoglobin: an example/model of an allosteric protein.
  6. Enzymes: the theory of enzyme catalysis; fundamentals of enzyme kinetics; regulation of enzyme activity.
  7. Mechanisms of enzyme action: acid-base and covalent catalysis. Coenzymes.
  8. Thermodynamic foundations and strategy of metabolism.
  9. Glycolysis. Pentose phosphate pathway and gluconeogenesis. Glycogen metabolism.
  10. Citric acid cycle.
  11. Oxidative phosphorylation.
  12. Metabolism of fats and fatty acids.
  13. Metabolism of amino acids and urea cycle.
  14. Nucleic acids: conformation and conformational stability of DNA and RNA; conformational transitions in DNA; interactions of DNA with ligands (small molecules, proteins).
  15. Expression and transmission of genetic information.

Labwork:

7 points (3 hours a week)

Syllabus:

  • Chromatographic techniques of protein separation.
  • Electrophoresis of selected proteins.
  • Reversible denaturation of proteins.
  • Hemoglobin: an introduction to its basic properties.
  • An introduction to basic properties of enzymes.
  • Determination of the activity of selected enzymes.
  • Determination of the basic parameters of enzyme kinetics.
  • Bioenergetics and strategy of metabolism (theoretical exercise).
  • Glycolysis and fermentation in yeast.
  • Isolation, purification and spectral characterization of DNA.

Colloquia:

35 points

Written exam:

15 points

Oral exam:

40 points