SubjectsSubjects(version: 982)
Course, academic year 2026/2027
  
   
Biochemistry A - B320001
Title: Biochemie A
Guaranteed by: Department of Biochemistry and Microbiology (320)
Faculty: Faculty of Food and Biochemical Technology
Actual: from 2026
Semester: winter
Points: winter s.:6
E-Credits: winter s.:6
Examination process: winter s.:
Hours per week, examination: winter s.:3/2, C+Ex [HT]
Capacity: unknown / unknown (unknown)Schedule is not published yet, this information might be misleading.
Min. number of students: unlimited
State of the course: taught
Language: Czech
Teaching methods: full-time
Level:  
Additional information: https://e-learning.vscht.cz/course/view.php?id=3290
Note: course can be enrolled in outside the study plan
enabled for web enrollment
Guarantor: Hynek Radovan prof. Dr. Ing.
Classification: Chemistry > Biochemistry
Interchangeability : AB320001
Is pre-requisite for: B319009, B320002, B319001
Is interchangeable with: AB320001, B320001X
In complex pre-requisite: B320005
Examination dates   Schedule   
Annotation -
This course will open the way for you to understand the nature of life at the molecular level. You will learn the basics of biochemistry and biochemical thinking. In the first part, you will learn about the properties of various biological molecules, including the connections between their structure and function. You will also learn about the methods used in biochemistry to characterize biomolecules. You will also learn about the principles of enzyme catalysis and the division of enzymes into basic classes, the function of biomembranes and membrane transport. In the next part, you will gain insight into the general principles of substance and energy conversion, and you will learn about the main metabolic pathways, including photosynthesis and the metabolism of nitrogenous substances. Completing the course will allow you to understand the functioning of living organisms and their mutual cooperation in a deeper way.
Last update: Hynek Radovan (25.04.2025)
Course completion requirements -

Attendance at lectures is recommended but not monitored.

Last update: Hynek Radovan (25.04.2025)
Literature -

Obligatory:

  • Kodíček, Milan, Valentová, Olga, Hynek, Radovan. Biochemie, chemický pohled na biologický svět. : , , https://vufind.techlib.cz/Record/001877049 s. ISBN 978-80-7592-124-6.

Optional:

  • Hames, B.D., Hooper, N.M.. Biochemistry. Oxford: Bios, 2000, 422 s. s. ISBN 1-85996-142-8.
  • Voet, Donald, Voet, Judith G., Pratt, Charlotte W.. Principles of biochemistry. Hoboken: Wiley, 2008, 1099 s. s. ISBN 978-0470-23396-2.
  • Berg, Jeremy M., Tymoczko, John L., Stryer, Lubert, Gatto, Gregory J., Jr.. Biochemistry. New York: W. H. Freeman, 2012, s. ISBN 1-4292-7635-5.

Last update: Hynek Radovan (25.04.2025)
Teaching methods -

Biochemistry I is a fundamental theoretical course. Students primarily acquire basic knowledge in the field of biochemistry through lectures that include practical aspects of applying this knowledge in real life. During the course, methods are used to verify the understanding of the material, such as quiz tests or group problem-solving. Additionally, after each lecture, an e-learning test is available to review the knowledge gained from the lecture.

Last update: Hynek Radovan (25.04.2025)
Requirements to the exam -

Course with Exam and Credit:

The exam consists of a written and an oral part.

The written part is mandatory, and the oral part can only be taken after obtaining at least 50 points from the written part (up to 10 points from self-testing in the e-learning course can be added to the written part score). If less than 50 points are achieved, the exam is graded F.

The written part consists of ten questions, each graded 0–10 points. If the oral part is unsuccessful, the written part must be retaken.

The condition for awarding credit is passing two interim written tests.

Credit is awarded if an average of at least 50 points is achieved from both interim written tests (each test is graded 0–100 points). The student has two additional attempts to achieve 50% on the credit test.

The final grade is determined by the weighted average of two values:

Points from the written part, including bonus points from e-learning (weight 50%).

Points from the oral exam (weight 50%).

However, if the exam is graded F, the final grade is also F.

Last update: Hynek Radovan (25.04.2025)
Syllabus -

1. Definition of biochemistry and its position in the system of natural sciences. Organization of living systems. Amino acids (properties, reactions), peptides.

Define what biochemistry deals with. Composition and organization of living systems, molecular recognition. Types of non-covalent interactions. Define the differences between prokaryotes and eukaryotes; also the differences between plant and animal cells. Proteinogenic amino acids - names, formulas, 3-letter codes, properties, titration curves, calculations of isoelectric points. Peptide bond - formula of a polypeptide chain, peptide nomenclature, calculation/estimation of isoelectric points for simple peptides.

2. Proteins, classification and general functions of proteins. Levels of structures, properties, relationship of structure and function.

Functions of proteins and peptides in living organisms. Description of the level of protein structures. Be able to explain denaturation. Common covalent modifications of proteins, namely disulfide bridges, phosphorylation and glycosylation. Examples of the relationship between the structure and function of proteins (difference between the saturation curve of hemoglobin and myoglobin).

3. Methods used for biochemical characterization of living organisms (chromatography, electromigration techniques, immunochemical techniques, mass spectrometry, PCR).

Principle of separation using GPC, IEC, affinity chromatography. Electrophoretic methods SDS-PAGE, IEF. Basic types of ELISA, Edman degradation, PCR. Basic types of mass spectrometry used in biochemistry (MALDI-TOF, LC-MS/MS).

4. Enzymes: structure, terminology, classification.

Explain the principles of enzyme catalysis and comparison with non-enzymatic catalysts. Specificity of enzymes. Know that there are classes of enzymes. Know what cofactors are and their relationship to vitamins. Define the difference between a coenzyme and a prosthetic group.

5. Reaction kinetics of enzyme reactions and types of inhibition.

Define the initial reaction rate. Write the Michaelis-Menten equation, define its parameters and their significance. Explain different types of enzyme inhibition. Allosteric effect (allosteric inhibition and activation).

6. Principles of substance and energy transformation and bioenergetics.

Definition of metabolism. Describe the steady state. Basics of the division of organisms in terms of nutrition (trophics). Difference between aerobic and anaerobic organisms. Relationship between autotrophs and heterotrophs. Explain what catabolism, anabolism and their mutual relationship are. Types of metabolic pathways. Role of ATP in metabolism and methods of its synthesis.

7. Citrate cycle. Aerobic and anaerobic respiration.

Intracellular localization of TCA. Summary equation. Position in catabolism. Connection to TCA – where reduced cofactors are regenerated. Sources of acetylCoA: connection with β-oxidation of fatty acids, oxidative decarboxylation. Amphibolic aspects of TCA reactions. The importance and position of TCA in metabolism. The position of the respiratory chain in metabolism. The principle and importance of respiration. The difference between aerobic and anaerobic respiration. What is the proton motive force, how is it formed and what are its units. The coupling of the respiratory chain and ATP synthesis by oxidative phosphorylation. The formation of ATP by photophosphorylation

8. Carbohydrates and their metabolism.

Definition of carbohydrates, function of carbohydrates, structure of the most important mono-, di- and polysaccharides. Catabolism and anabolism of carbohydrates (basics of glycolysis, pentose cycle, glycogenesis, glycogenolysis, glucogenesis). Important reactions of glycolysis, energy balance.

9. Photosynthesis – light phase, dark phase. C3, C4 and CAM plants.

The principle of photosynthesis and its summary equation. Description and localization of photosynthesis in higher green plants. Occurs in the light phase. Dark phase (Calvin cycle) in C3 plants. Differences in primary carbon dioxide fixation in C4 and CAM plants.

10. Lipid chemistry, biological membranes.

Definition of lipids, distribution and function. Structure and function of biological membranes. Properties of membranes.

11. Basics of transport through biological membranes.

Electrochemical potential. Active and passive transport. Activation of fatty acids. Pendulums for the transport of reduced cofactors. Symport, antiport, ATP pumps.

12. Lipid metabolism. Glyoxylate cycle.

Beta-oxidation of fatty acids and connection to TCA. Synthesis of fatty acids. Metabolism of ketone bodies. Basics of isoprenoid metabolism.

Summary equation, occurrence and importance of the glyoxylate cycle.

13. Metabolism of nitrogenous substances.

Protein catabolism. Function of proteolytic enzymes, division of amino acids into glucogenic, ketogenic and glucoketogenic. Classification of animal organisms according to nitrogen elimination (ureotelic, uricotelic and ammonotelic organisms), Ornithine cycle. Nitrogen metabolism in plants.

14. Chemistry of nucleic acids and their structure. Replication, transcription, translation and post-translational modification.

Components of nucleic acids and their role in the organism. Terminology – nucleotide, nucleoside, base. Base pairing. Purine and pyrimidine bases. Know the difference between purine and pyrimidine bases. Structure of prokaryotic and eukaryotic DNA (primary, secondary, tertiary). Structure of RNA (mRNA, rRNA and tRNA). Describe replication, transcription and post-transcriptional modifications. Difference between prokaryotes and eukaryotes. What are introns and exons. What is splicing. Explain what is the genetic code. Describe translation. What is a codon and anticodon. What are ribosomes. Basics of their composition (two subunits).

Last update: Hynek Radovan (25.04.2025)
Learning resources -

Materials for Biochemie I (Czech version) on: https://e-learning.vscht.cz/

Last update: Hynek Radovan (25.04.2025)
Learning outcomes -

Basic knowledge of biochemistry: Understanding the basic principles and processes of biochemistry, including the structure and function of biomolecules (proteins, carbohydrates, lipids, nucleic acids).

Ability to define and explain key biochemical concepts and processes. Gain theoretical knowledge in modern laboratory methods, including chromatography, electrophoresis, PCR, mass spectrometry.

Understanding the basics of enzyme catalysis. Knowledge of basic metabolic pathways.

In summary - understanding the functioning of living organisms at the molecular level.

These outcomes help students gain a solid foundation in biochemistry and prepare them for further study or a career in the chemical sciences.

Last update: Hynek Radovan (25.04.2025)
Entry requirements -

Organic chemistry I or Organic chemistry A

Last update: Hynek Radovan (25.04.2025)
Registration requirements -

Knowledge in Organic Chemistry I or Organic Chemistry A.

Last update: Lipovová Petra (16.05.2025)
Teaching methods
Activity Credits Hours
Účast na přednáškách 1 28
Příprava na přednášky, semináře, laboratoře, exkurzi nebo praxi 0.7 20
Práce na individuálním projektu 0.5 14
Příprava na zkoušku a její absolvování 1.4 40
Účast na seminářích 1 28
Semester tests 0.4 10
5 / 6 140 / 168
Coursework assessment
Form Significance
Homework preparation 10
Examination test 30
Continuous assessment of study performance and course -credit tests 30
Oral examination 30

 
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