Course code:
HF1BMOL		 Course name:
Structure of Biomolecules

Academic year:

2026/2027.

Attendance requirements:

There are no requirements.

ECTS:

5

Study level:

graduate academic studies

Study program:

Master 4.0 Bioinformatics: 1. year, winter semester, elective (M4B-E1) course

Teachers:

Tanja D. Ćirković Veličković, Ph.D.
full professor, Faculty of Chemistry, Studentski trg 12-16, Beograd

Dragana J. Stanić-Vučinić, Ph.D.
principal research fellow, Faculty of Chemistry, Studentski trg 12-16, Beograd

Marija M. Stojadinović, Ph.D.
assistant professor, Faculty of Chemistry, Studentski trg 12-16, Beograd

Assistant:

Višnja D. Jovanović
junior research assistant, Innovation center, Studentski trg 12-16, Beograd

Hours of instruction:

Weekly: two hours of lectures + two hours of exercises (2+2+0)

Goals:

The goal of this course is to introduce students to the basics of the science of living systems, with a focus on the structure and function of biomolecules that make up living nature: proteins, nucleic acids, lipids and sugars.

Outcome:

Students acquire competencies that enable them to understand the structure, function and interactions of biomolecules (proteins, nucleic acids, lipids, saccharides).

Teaching methods:

Lectures, practical classes, colloquium.

Extracurricular activities:

—

Coursebooks:
  • Lehninger: Principles of Biochemistry, W. H. Freeman and Co, 2005.
  • M. Zlatović, D. Petrović: Osnovi molekulskog modelovanja, praktikum, HeÜijski fakultet Univerzitet u Beogradu, 2016, ISBN 978-86-7220-078-2

Additional material:

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  Course activities and grading method

Lectures:

10 points (2 hours a week)

Syllabus:

  1. Definition, subject of study and multidisciplinary character of life sciences. Hierarchical organization of living systems.
  2. Chemical and physical foundations of life. The role of water and minerals in the functioning of living systems. Exchange of matter and energy in the cell.
  3. Information transfer in living systems. Origin of life and evolution.
  4. Amino acids, peptides and proteins. Levels of structural organization of proteins.
  5. Methods for determining the structure of proteins (from amino acid sequence to multimeric complexes).
  6. Basics of physiological activity of peptides. Classification of proteins.
  7. Nucleosides, nucleotides and classes of nucleic acids.
  8. Structure, physiological role and application of nucleotides and nucleic acids.
  9. Sugars: basic information on monosaccharides and disaccharides.
  10. Polysaccharides. Structure and function.
  11. Glycoconjugates. Structure and biological significance.
  12. Basic classes of lipids. Structure of the main representatives.
  13. Function of the main representatives of different classes of lipids.
  14. Structure of biological membranes and transport.
  15. Molecular mechanisms of signal transduction (Biosignaling).

The literature study will be conducted according to the Journal Club model, or rather a discussion forum, where students, together with teachers, analyze current scientific publications relevant to the topic.

Exercises:

10 points (2 hours a week)

Syllabus:

Exercises are done theoretically and involve: 1) basics of working with biomolecules and solving problems, 2) application of computer methods in processing experimentally obtained data on the structure and interactions of biomolecules:

  1. Determination of mass and isoelectric point of proteins by computer methods. Comparison with experimentally obtained data.
  2. Determination of secondary structure in proteins. Analysis of CD spectra of proteins using software.
  3. Software prediction of tertiary structure of proteins and comparison with experimental values; Ab initio modeling of the tertiary structure of proteins, as well as the structures of protein-protein and protein-nucleic acid complexes based on experimental results obtained by SAXS (Small Angle X-Ray Scattering) and SANS (Small Angle Neutron Scattering) techniques.
  4. Monitoring of protein conformational changes by CD spectroscopy, spectrofluorimetry, SAXS and SAXS techniques. Spectral analysis.
  5. Determination of ligand binding constants for proteins by modern methods. Mathematical modeling of experimentally obtained data.
  6. Processing of measurement results in determination of the melting point of proteins and nucleic acids.

Colloquia:

30 points

Practical exam:

50 points