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ЗмістQuestions for Module 2 P.69-71
4. Which amino acid can participate in disulphide bond formation?
The main theoretical questions
Sequence of procedure
Biuret reaction: Sequence of procedure
1. Which of the following reagents can denature proteins?
3. Which one of the following statements concerning phenylalanine is correct?
4. Which amino acid is hydrophobic?
6. The primary structure of protein is stabilized by
8. Which one of the following statements concerning primary structure of protein is correct?
9. Which one of the following statements concerning secondary structure of proteinis correct?
10. Which one of the following statements concerning tertiary structure of protein is correct?
The methodical guidelines for practice activity on the theme
The investigation of enzymes structure, physical-chemical properties and conditions of action.
The main theoretical questions
Study of enzyme thermolability»
«definition of amylase and sucrase specificity»
Table of contents
Module 2. The common mechanisms of metabolism. Metabolism of carbohydrates, lipids and proteins. Regulation.
Substantial module 2. 1. The role of enzymes and vitamins in metabolism"
Topic 2.1. The control of original knowledge level. Subject and task of biochemistry.
The investigation of protein structure and physical-chemical properties.
Quantitative definition of protein by the biuretic method. The proof of protein
nature of enzymes. ……............................................................................... P.3-6
Topic 2.2. The investigation of enzymes structure, physical-chemical properties and
conditions of action ………………………………………………………….. P 7-9.
Topic2.3. Determination of enzyme activity. Investigation of enzyme catalysis kinetics …..P.10-12
and activators and inhibitors influence on enzyme activity.
Topic 2.4. Investigation of the vitamins coenzyme form role in catalytic enzymes activity. P.13-15
Topic 2.5. Investigation of the vitamins and vitamins coenzyme form function ……………...P.16-18
In different biochemical processes.
Substantial module 2. 2“ Basic concepts of metabolism, bioenergetics.
Topic 2.6. Investigation of oxidative phosphorylation and ATP synthesis. Inhibitors ………P.19-22
and uncouples of oxidative phosphorylation.
Topic 2.7. Bioenergetics and general pathways of a metabolism. The investigation of…….. P.23-25
citric acid cycle action.
Substantial module 2. 3 “Metabolism of carbohydrates, its regulation”.
Topic 2.8. Investigation of carbohydrate digestion peculiarities. Glycogen biosynthesis P. 26-29
and degradation. Conversion of monosacharides to glucose in the liver.
Topic 2.9. Anaerobic oxidation of carbohydrates. Glycolysis. Synthesis of glucose –
gluconeogenesis. ……………………………………………………………… P. 30-32
Topic 2. 10 Investigation of aerobic oxidation of glucose. Pentose phosphate pathway….. P. 33-35
of glucose conversion.
Substantial module module 2. 4“Metabolism of lipids, its regulation”.
Topic 2. 11 Structure and functions of cellular membranses. P.36-40
Topic 2. 12 Investigation of lipids digestion peculiarities. Possible disturbanses of P. 41-44
exogenic lipids digestion, absorbtion and transtort.
Topic 2. 13 Investigation of fatty acids and keton bodies metabolism. β-oxidation of fatty P. 45-49
acids. Cholesterol synthesis and steroid metabolism. Disturbances of lipid
metabolism atherosclerosis. Topic 2. 14 Investigation of fatty acids, triacylglycerol and phospholipid synthesis. ….. P. 50-52 Disturbances of lipid metabolism: obesity; lipid dystrophy of the liver.
Substantial module 2. 5 “Metabolism of amino acids, its regulation”.
Topic 2.15 Investigation of gastric juice chemical composition. Studies of proteins P. 53-57
Topic 2. 16. Studies of amino acids transformation (deamination, transamination…………. P.58-65
decarboxylation) Investigation of separate amino acid metabolism pathways.
synthesis. Disturbances of amino acid metabolism
Topic 2. 17 Investigation of ammonia detoxication and urea synthesis mechanisms. P. 66-68
Task for control module preparing. P.72-75
Topic 2.1. THE METHODICAL GUIDELINES FOR PRACTICE ACTIVITY ON THE THEME:
The control of initial knowledge level. Subject and task of biochemistry. The investigation of protein structure and physical-chemical properties. Quantitative definition of protein by a biuretic method. The proof of protein nature of enzymes.
Thousands of proteins present in the human body perform functions too numerous to list. These include serving as carriers of vitamins, oxygen, and carbon dioxide plus structural, kinetic, catalytic, and signaling roles. It thus is not surprising that dire consequences can arise from mutations either in genes that encode proteins or in regions of DNA that control gene expression. Consequences equally adverse can also result in deficiency of cofactors essential for maturation of a protein. Ehlers-Danlos syndrome illustrates a genetic defect in protein maturation and scurvy a deficiency of a cofactor essential for protein maturation Gross changes in the secondary-tertiary structure of proteins that occur independently of changes in primary structure also are responsible form major diseases. Diseases characterized by significant alterations in secondary-tertiary structure include the prion diseases Creutzfeldt-Jakob disease, scrapie, and bovine spongiform encephalopathy ("mad cow" disease), each characterized by pathologic neurological changes that result from deposition of insoluble proteins in amyloid fibrils composed of continuously hydrogen-bonded β-sheets.
Proteins play the central role during living of cells and forming of the cellular structures. The analysis of the contents in blood of the certain proteins and enzymes is widely used in the diagnostic purposes. At diseases of a liver diagnostic inspection by all means includes electrophoretic definition of the relative contents of albumins and globulins in the plasma of blood. The analysis of the contents lipoproteins and antibodies is usually used at diagnostics of specific types hypoproteinemia and immune infringements. Detection even small amounts of fiber serve in urine the important parameter of disease of kidneys.Now familiarize with the purpose of occupation, think over them, acquire necessity of their studying.
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Види занять з дисципліни: Курс теорії перекладу складається з лекційних годин та самостійної роботи