Course code:
401B1		 Course name:
Biochemistry of Proteins and Nucleic Acids

Academic year:

2019/2020.

Attendance requirements:

101A1 + 201B1

ECTS:

12

Study level:

basic academic studies

Study program:

Biochemistry: 2. year, winter semester, compulsory course

Teacher:

Natalija Đ. Polović, Ph.D.
full 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

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

Hours of instruction:

Weekly: four hours of lectures + seven hours of labwork (4+0+7)

Goals:

The goal of this course is to help students acquire fundamental knowledge of the structure and function of proteins and nucleic acids. Students should understand the connection between the structure and function of proteins and nucleic acids. This course provides students with a foundation for biochemistry and molecular biology courses in the subsequent years of their studies. Students will become familiar with the basic techniques and methods used for isolation and characterization of proteins and nucleic acids and they will acquire the basic skills necessary for working in a biochemical laboratory.

Outcome:

Understanding the structure of proteins and nucleic acids, the connection between the structure and activity of proteins and the relationship between proteins and nucleic acids at the level of undergraduate studies. Acquired basic skills necessary for working in a biochemical laboratory and developed initial understanding of experimental work with proteins and nucleic acids.

Teaching methods:

Lectures, experimental exercises, theory exercises, individual and group work with students on consolidating the course units.

Extracurricular activities:

—

Coursebooks:

Main coursebooks:

  • Vesna Niketic: Principi strukture i aktivnosti proteina
  • Vesna Niketic: Uputstva za vežbe
  • D. Voet, J. Voet: Biochemistry, 2004.
  • C. R. Calladine, H. R. Drew: Understanding DNA

Supplementary coursebooks:

  • Natalija Polović: PPT presentations
  • D. L. Nelson, M. M. Cox, Lehninger: Principles of Biochemistry
  • J. M. Claviere, C. Notredame: Bioinformatics for Dummies, Wiley, 2007.
  • Selected original papers from current literature
  • Web pages relevant to this course

Additional material:

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  Course activities and grading method

Lectures:

2 points (4 hours a week)

Syllabus:

  • Introduction.
  • The relationship between proteins and nucleic acids.
  • Amino acids.
  • The peptide bond.
  • Methods for working with proteins.
  • The primary structure of proteins; post-translational modifications of proteins; the evolution (history) of proteins.
  • The secondary structure of proteins.
  • Fibrous proteins.
  • The tertiary structure of globular proteins (conformational stability; supersecondary structures and domains).
  • Conformational transitions of proteins.
  • Flexibility and dynamics of protein structure.
  • Predicting protein structure.
  • The quaternary structure of proteins.
  • Protein activity: protein-ligand interactions at equilibrium (dependent and independent centers).
  • The regulation of biological activity: the cooperative effect in hemoglobin.
  • Nucleic acids: structure and dynamics (Introduction).
  • The chemical structure of nucleic acids.
  • Properties of bases, nucleosides and nucleotides.
  • Nucleic acid probes: sequence determination, the secondary and tertiary structure of DNA and RNA.
  • Conformational analysis and factors which determine the structure of nucleic acids.
  • The standard (canonical) structure of DNA and the structure which depends on the base sequence.
  • Conformational transitions of DNA.
  • Interactions of DNA with ligands.
  • The tertiary structure of RNA.
  • RNA-protein interactions.

Labwork:

15 points (7 hours a week)

Syllabus:

  • Safety in biochemical laboratories and handling biological material.
  • Aqueous solutions (preparation of solutions of given concentrations).
  • Laboratory buffers.
  • Amino acids.
  • Basic chemical and physical properties of proteins.
  • Determining the concentration of proteins.
  • Gel filtration and ion exchange chromatography of proteins.
  • SDS-electrophoresis of proteins.
  • Introduction to bioinformatics.
  • Protein-ligand interactions.
  • Biochemistry of protein folding.
  • Isolation of DNA from biological material.
  • Spectral characterization of the isolated DNA.

Semester papers:

3 points

Colloquia:

30 points

Written exam:

20 points

Oral exam:

30 points