COURSE OBJECTIVE:
Introducing students to the molecular logic of biochemical processes in a living organism and the dynamics of synthesis and degradation of natural biomacromolecules: proteins, polysaccharides, lipids and nucleic acids. The principles of cellular metabolism and the principles of regulation and control are studied.
COURSE IMPLEMENTATION PROGRAM:
WEEK 1
Introduction - Biochemistry as a science, the connection between natural and biomedical knowledge,
proteins - diversity of protein and peptide functions, amino acid protein structure, peptide bond, conformation, dynamic aspects of protein structure and function, research foundations and principles of protein isolation.
WEEK 2
Proteins with special functions - hemoglobin, model globular protein, interactions of hemoglobin with ligands, structure, function and regulation, allosteria cooperative oxygen binding, myoglobin.
WEEK 3
Differences between monomers and tetramers. Fibrillar proteins - collagen, elastin.
WEEK 4
Enzymes and bases of enzyme catalysis - regulation of activity of metabolically important enzymes - strategy and mechanisms, allosteric regulation of enzyme activity, activators and inhibitors, coenzymes and prosthetic groups: structure and function, proteins that bind to DNA.
WEEK 5
Generation and storage of metabolic energy: metabolism - basic concepts and properties. Metabolic glucose degradation - metabolic pathway, control and regulation, allosterically regulated enzymes, hexokinase, phosphofructokinase, pyruvate kinase, ATP production, importance of NADH oxidation and LDH reaction.
WEEK 6
Gluconeogenesis - non-carbohydrate metabolic precursors of glucose, differences in glycolysis and gluconeogenesis, biotin and carboxylation, the role of oxaloacetate, regulation of glycolysis and gluconeogenesis is reciprocal, Cori cycle and lactate utilization, energy consumption in gluconeogenesis, fruconeogenesis.
WEEK 7
Oxidative decarboxylation of pyruvate, citric acid cycle. The formation of acetyl-CoA from pyruvate, the pyruvate dehydrogenase-coenzyme and prosthetic group complex, citrate synthesis and review of citric acid cycle reactions, energy changes in reactions and flow control, the cycle is a source of biosynthetic precursors and energy for the cell, anaplerotic cycle intermediate replenishment reactions.
WEEK 8
Cellular bioenergetics, ATP cycle, respiratory chain and oxidative phosphorylation. Redox potentials and free energy change, inner mitochondrial membrane and localization of respiratory multienzyme complexes, cascade oxidation of coenzymes NADH and FADH2 oxygen is the ultimate acceptor of H + and electrons, proton pumps and H + gradient formation, connection with phosphorylation and synthesis of ATP-ATP syntha , energy efficiency of complete glucose oxidation, regulation of oxidative phosphorylation.
WEEK 9
Pentose phosphate pathway direct oxidation of glucose and formation of ribose-5-phosphate and NADPH. Transaldolase and transketolase link the pentose phosphate pathway and glycolysis.
WEEK 10
Glycogen metabolism: glycogenesis and glycogenolysis, course and hormonal regulation. Phosphorylase and phosphorolytic degradation of glycogen, enzymes for removing branches, Synthesis of UDP-glucose. Hormonal regulation of synthesis and degradation. Enzyme phosphorylation reaction cascade and control, cAMP. Glycogen metabolism in the liver and control of blood glucose concentration.
WEEK 11
Fat metabolism: degradation of triacylglycerol, b-oxidation of fatty acids, biosynthesis of fatty acids, biosynthesis of triacylglycerol. urea cycle, control enzymes and energy expenditure in the urea cycle, the link between the urea cycle and the citric acid cycle, the mechanism of NH4 + ion toxicity in the brain.
WEEK 12
Amino acid metabolism. Amino acid degradation and the urea cycle. Transamination and degradation of amino acids, reaction mechanism and role of pyridoxal phosphate in amino acid transamination, serine and threonine dehydrate, fate of C-atoms of degraded amino acids, C-3, C-4 and C-5 families, degradation of branched chain amino acids and aromatics , ketogenic amino acids, biosynthesis of non - essential amino acids, serine, glycine.
WEEK 13
Nucleic acids - structure, function of biosynthesis and degradation. Nucleotide structure, structure, biosynthesis of purine and pyrimidine bases, synthesis of deoxyribonucleotides, degradation of purine bases and uric acid synthesis, degradation of pyrimidine, properties and replication of DNA, structure and types of RNA genetic information.
WEEK 14
Information in biological systems. DNA - genetic role, structure, genome organization, chromosomes and genes. DNA packaging and histones. DNA conformations. DNA replication, replication fidelity. DNA defects and their repair. RNA in the creation and translation of the genetic message. Synthesis and modification of functional RNA molecules: mRNA and transcription, t-RNA, activation and role in protein synthesis, ribosome structure and rRNA.
WEEK 15
Genetic code and gene-protein relationships. Protein synthesis. Control of gene expression in prokaryotes: Lac-operon and Trp-operon. Eukaryotic chromosomes and control of eukaryotic gene expression. Meaning of introns and exons.
DEVELOPMENT OF GENERAL AND SPECIFIC COMPETENCIES OF STUDENTS:
After completing the course, the student acquires the ability to think critically about biochemical processes and metabolic reactions in various organs and tissues that are important for understanding physiological and pathological processes.
STUDENTS 'TEACHING OBLIGATIONS AND THEIR PERFORMANCE:
Students are required to submit 2 assignments via e-learning.
CONDITIONS FOR TAKING THE EXAM:
Committed 2 assignments via e-learning.
TEACHING METHODS:
Lectures (ex cathedra, ex camera).
Seminars (ex cathedra, ex camera).
Consultations by arrangement with students.
METHOD OF EXAMINATION OF KNOWLEDGE AND EXAMINATION:
3 mandatory written tests during the semester (60% of points on each of the tests brings exemption from the oral exam).
Written exam (requires 50% points to pass).
Oral exam.
METHOD OF MONITORING THE QUALITY AND PERFORMANCE OF COURSES:
Student survey.
METHODOLOGICAL PREREQUISITES:
Passed exams from the 1st academic year and Organic Chemistry I, and attended the course Organic Chemistry II.
COURSE LEARNING OUTCOMES:
1. Explain and connect biochemical processes and metabolic reactions in different organs and tissues
2. Interpret the conditionality of three-dimensional structure and biological activity on the example of proteins.
3. Discuss the creation and storage of metabolic energy, and the overall metabolism strategy.
4. Define the basic principles and importance of the central dogma of molecular biology and the basic concepts related to the formation and structure of nucleic acids in living organisms.
5. Explain the mechanisms of DNA replication, DNA transcription and RNA translation.
LEARNING OUTCOMES AT PROGRAM LEVEL:
1. Solve qualitative and quantitative problems by applying appropriate chemical principles and theories
2. To interpret chemical information and data
3. Search for information available on the Internet
4. To apply knowledge in practice, especially in problem solving based on qualitative or quantitative information
5. To demonstrate the ability to engage in interdisciplinary teamwork
TEACHING UNITS
1. Conformation and dynamics. Conditionality of three-dimensional structure and biological activity on the example of proteins. Myoglobin and hemoglobin. Enzymes. Collagen and elastin.
Learning outcomes:
- recognize the connection between natural and biomedical knowledge
- compare the diversity of protein and peptide functions
- determine the amino acid structure of proteins, peptide bond, conformation, dynamic aspects of protein structure and function
- distinguish proteins with special functions, hemoglobin, model globular protein and interactions of hemoglobin with ligands, and myoglobin
- understand the conditionality of the structure and function of fibrillar proteins collagen and elastin
- know the basics of enzyme catalysis, allosteric regulation of enzyme activity, activators and inhibitors, coenzymes and prosthetic groups
Evaluation criteria:
- know how to write the structures of all 20 amino acids
- define the structure of complex proteins, from primary to quaternary
- apply knowledge of the structure and function of proteins to hemoglobin and myoglobin, and fibrillar proteins collagen and elastin, as proteins with special functions
- know the regulation of the activity of metabolically important enzymes, coenzymes and prosthetic groups
2. Generation and storage of metabolic energy. Overall metabolism strategy.
Learning outcomes:
- explain the basic concepts and properties of metabolism
- understand the metabolic breakdown of glucose - the course of the metabolic pathway, control and regulation, allosterically regulated enzymes, ATP production, the importance of NADH oxidation
- sketch the cycle of gluconeogenesis, the citric acid cycle, the Cori cycle
- explain cellular bioenergetics, ATP cycle, respiratory chain and oxidative phosphorylation, cascade oxidation of coenzymes NADH and FADH2
- write the basic stages of fat metabolism: the breakdown of triacylglycerol and b-oxidation of fatty acids
- compare in the urea cycle different ways of excretion of nitrogen from the body, alanine and glutamine cycle of nitrogen transfer from various tissues in the liver, oxidative deamination of glutamate, urea cycle, and the mechanism of toxicity of NH4 + ions in the brain
Evaluation criteria:
- notice differences in the stages of individual metabolic cycles
- know common precursors of several cycles, and input and output components
- apply knowledge of the overall metabolism strategy to each individual cycle
3. Central dogma of molecular biology.
Learning outcomes:
- define the basic principles and importance of the central dogma of molecular biology
- explain the formation of nucleic acids in living organisms
- define higher structural forms of DNA in prokaryotes and eukaryotes
- explain the mechanisms of DNA replication, DNA transcription and RNA translation
Evaluation criteria:
- explain the concept and importance of the central dogma of molecular biology in their own words
- know the way in which nucleic acids are formed in living organisms
- know the way of formation of higher structural forms of DNA in prokaryotes and eukaryotes
- understand the mechanisms of DNA replication, DNA transcription and RNA translation
- notice the difference between DNA replication, DNA transcription and RNA translation
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