Biochemistry – English programme – Faculty of Medicine
Winter semester 20014/2015
No
Tuesday
Topic
Thursday
30.IX
7.X.
2.X.
9.X.
14.X.
16.X.
3.
4.
5.
6.
Introduction to classes
Amino acids, peptides, proteins – structure, properties,
function
Purine and pyrimidine nucleotides. Structure and
function of nucleic acids.
Biosynthesis of protein
Enzymes – general properties, kinetics
Enzymes – regulation of activity
Dietary proteins, protein digestion
21.X.
28.X.
4.XI.
23.X.
30.X.
6.XI.
13.XI.
*
Re-sit – topic number – 1,2, 3, 4, 5, 6,
18.XI.
20.XI.
7.
8.
Plasma proteins. Immunoglobulins
Biosynthesis of the nutritionally nonessential amino
acids. Conversion of amino acids to specialized product
Catabolism of amino acid nitrogen. The urea cycle
The citric acid cycle.
25.XI.
2.XII.
27.XI.
4.XII.
9.XII.
16.XII.
11.XII.
18.XII.
1.
2.
9.
10.
*
11.
*
Winter holiday
11.XI. Independent
Day,
Test on seminar
12.XI.
24.XII. 2014 – 6.I. 2015
Biologic oxidation. The respiratory chain
13.I.
15.I.
Re-sit – topic number – 7, 8, 9, 10, 11
20.I.
22.I.
Semester
29.09.2014 – 27.01.2015
Session
28.I. – 10.II. 2015
Term break
11 – 18.II. 2015
Rector days
4.X., 10.XI. 2014
Exam 25.06.2015; Checking the tests 30.06.2015
Harper’s Ilustrated Biochemistry, 29 th edition (black)
1. Amino acids, peptides, proteins
Ch. 3 ; 5
Biomedical importance of amino acids. Properties of amino acids. Isoelectric point. Functions of side chains of
amino acids . Biomedical importance of peptides. Classification and nomenclature of peptides. Biomedical
importance of proteins. Classification of proteins. Higher orders of protein structure. The bonds which stabilize
protein structure. Protein properties. The features of protein in isoelectric point. Protein folding. Pathologic
consequences as a result of perturbation of protein conformation. Characteristic features of collagen structure.
Impairment in collagen maturation. Posttranslational modification of proteins.
2. Nucleotides. Nucleic acids structure and function.
Ch. 32 ; 34
Biomedical importance of nucleotides. Chemistry of purines, pyrimidines, nucleosides and nucleotides.
Physiologic functions of nucleotides. Synthetic nucleotide analogs. Polynucleotides. Biomedical importance of
nucleic acids. Sructure and role of DNA. Denaturation of DNA. Differences between DNA and RNA. Types of
RNA and their functions. P bodies. Nucleases.
3. Biosynthesis of protein.
Ch. 37.
Biomedical importance. Characteristic of the genetic code. Features of the genetic code.
“Wobble “ hypothesis. Types of mutations and their consequences. Role of aminoacyl-tRNA synthetases. Role
of different types of RNA in protein biosynthesis. Three phases of translation. The role of the “cap” and poly(A)
“tail” in initiation of translation. The regulation of the rate of initiation of protein synthesis. Posttranslational
modification of proteins. The antibiotic influence on protein synthesis.
4. Enzymes – mechanism of action, kinetics.
Ch. 7; 8
Biomedical importance of enzymes. Classification and nomenclature of enzymes. Coenzymes, prosthetic groups
and cofactors. Significance of metal ions in substrate binding and catalysis. Metalloenzymes and enzymes
activated by metals. Mechanisms of enzymatic catalysis. Isoenzymes. Serum enzymes used in clinical diagnosis.
Ribozymes. Theory of transient state. Specificity of enzymes reaction. Velocity of enzymatic reactions. Factors
affected velocity of enzymatic reactions. The kinetics of enzymatic catalysis. Active and allosteric site –
structure and importance. The Michaelis-Menten and Hill equations. Inhibition of enzymatic reactions.
Competitive and noncompetitive inhibition. Enzymes poisons. Types of enzymatic reactions.
5. Enzymes – regulation of activities
Ch. 9; 38
Biomedical importance. Regulation of metabolite flow. Compartmentation of enzymes. Rate-limiting reactions.
Regulation mechanisms of enzymes activity: regulation of enzymes quantity and catalytic efficiency.
Multienzymatic complexes. Allosteric effectors. Feedback inhibition. Covalent modification. Limited
proteolysis. Constitutive and inducible enzymes. Operon model. Inducer and repressors. Gratuitous inducer.
6. Protein digestion.
Ch. 43.
Biological value of proteins: high quality proteins, partial quality proteins, non quality proteins. Nitrogen
balance. Protein and amino acids requirements. Protein digestion. Specificity of proteases. Hydrochloric acid
production. Significance of hydrochloric acid and proteolytic enzymes in protein digestion. Regulation of
activity of proteases. Mechanisms of amino acids absorption. Significance of intestine bacteria in fermentation
process. Marasmus, kwashiorkor, cachexia.
7. Plasma proteins.
Ch. 50.
Biochemical importance of plasma protein. Division and functions of plasma proteins (apart of iron metabolism).
Plasma proteins properties. Plasma proteins significance in transport of hydrophobic substances. Colloidal
osmotic pressure in physiologic and pathologic condition. Proteins of acute phase. Amyloidosis.
Immunoglobulins: nomenclature, functions in protective mechanism of organism. Structure of immunoglobulin.
The role of Fab and Fc fragments of immunoglobulin molecules. Comparison of immunoglobulin classes. Class
switching. The complement system.
8. Biosynthesis of amino acids. Conversion of amino acids to specialized products.
Ch. 27; 30
Biomedical importance. Nutritionally essential and nonessential amino acids. Biosynthesis of nutritionally
nonessential amino acids. Conversion of L-α-amino acids to specialized products.
Conversion of non-α-amino acids to specialized products. Significance of these products in human organism.
9. Catabolism of proteins and amino acid nitrogen.
Ch. 28.
Biomedical importance. Turnover of proteins. Half-life of proteins. ATP-independent protein degradation. ATP
and ubiquitin-dependent degradation of proteins.
Interorgan exchange of amino acids. Deamination,
deamidation, transamination reactions: tissue localization and biochemical pathway. Reactions which release
ammonia. Cellular mechanism of ammonia detoxification. Role of glutamate dehydrogenase in: brain, liver and
kidney. Significance of liver and muscle in nitrogen metabolism of organism. Purine and alanine cycle. Urea
cycle. Metabolic disorders included with urea cycle reactions.
10. The citric acid cycle.
Ch. 11; 17
Biomedical importance of production and storage the energy in cells. Entrophy, enthalpy, exergonic and
endergonic reactions. High-energy phosphates. High-energy phosphates as the “energy currency” of the cell.
Biomedical importance of Krebs cycle. Characteristic of Krebs cycle reactions and their regulation. Energetic
balance of Krebs cycle. Roles of vitamins in citric acid cycle. Amphibolic role of Krebs cycle.
11. Biologic oxidation. The respiratory chain.
Ch. 12; 13
Biomedical importance of biologic oxidation. Redox potential. Characteristic of oxidases, dehydrogenases,
hydroperoxidases, oxygenases. Reactive forms of oxygen. Toxicity of oxygen. Specific role of catalase,
peroxidases and superoxide dismutase. Biomedical importance of respiratory chain. Characteristic of elements of
respiratory chain. The Q cycle. Electron transport via respiratory chain. Significance of proton pumps and
electrochemical gradient. Mechanism of ATP production by ATP synthase. Respiratory control. Poisons of
respiratory chain. Significance of uncouplers. Transporter system in the inner mitochondrial membrane.
Transport of substrates via the inner mitochondrial membrane.