Centrifugtion
1. Give 3 factors influencing centrifugal force.
2. Explain the term (abbreviation) RPM.
3. Explain the term (abbreviation) RCF.
4. Give factors influencing value of RCF.
5. What is more accurate description of conditions of the centrifugation: value of RPM or RCF? Why?
6. Explain the term „ultracentrifuge“.
7. Explain why a centriguge must be balanced.
8. Explain the term „differential centrifugation“.
9. What is a difference between an analytical and a preparative centrifugation?
10. Explain the term „supernatant“.
11. What particles will not be separated from liquid (e.g. blood plasma) under lower RPM (RCF)? Think
about size of the particles.
12. Why a centrifuge must be closed during centrifugation?
13. What centrifugal conditions are used to separate blood clot from serum? (RCF, time)?
Electrophoresis
1. Do anions move toward catode or anode?
2. Give at least 3 factors influencing velocity of ions during an electrophoretic separation.
3. How does an applied voltage influence velocity of ion movement?
4. Explain the term „amphoteric substance“ and give an example.
5. What is the charge of protein in a solution of pH  pI?
6. What is the charge of protein in a solution of pH = pI?
7. Give at least 3 examples of support medium used for electrophoresis.
8. Explain the abbreviation PAGE used in relation to electrophoretic techniques.
9. Explain the term „capillary electrophoresis“.
10. How many fractions are formed by separation of serum proteins using an agarose gel
electrophoresis?
11. Explain why does PAGE-electrophoresis separate proteins to more fractions in a comparision with
an agarose gel electrophoresis.
12. What type of current is used for electrophoresis, alternating or direct one?
13. How chart of electrophoresis patern (peaks) can be obtained? (the method)
14. Give at least 3 examples of use of the electrophoretic techniques.
15. Explain the term SDS-PAGE.
16. Explain the term „diffusion“.
Structure and metabolism of proteins (= examples of questions related to module B examination)
1. Draw general structure of -L-amino acid.
2. Explain the term „-carbon“.
3. Draw a peptide bond.
4. Make a definition of protein.
5. Explain the term „primary structure of protein“ and specify bonds which participate in it.
6. Explain the term „secondary structure of protein“ and specify bonds which participate in it.
7. Explain the term „tertiary structure of protein“ and specify bonds which participate in it.
8. Explain the term „quaternary structure of protein“ and specify bonds which participate in it.
9. Where are proteins synthesized within a cell?
10. Explain the term „proteinogenic amino acids“. Give their number.
11. Explain the term „posttranslational modification of proteins“. Give at least 3 examples.
12. Explain the term „O-glycosidic bond“. What amino acids can participate in it?
13. Explain the term „N-glycosidic bond“. What amino acid participates in it?
14. Explain the term „metalloprotein“ and give an example.
15. Explain the term „hemoprotein“ and give an example.
16. Explain the difference between the molecules: glycoprotein and proteoglycan.
17. Explain the term „lipoprotein“ and give an example.
18. Enumerate at least 5 functions of proteins of human body.
19. Enumerate functions of membrane proteins.
20. Explain the term „isoelectric point“.
21. What is the difference between albumin and globulin (see physicochemical properties)?
22. Give an example of fibrous protein.
23. What are factors influencing solubility of a protein?
24. What happens after addition of an acid to a protein solution?
25. Explain the term „protein denaturation“.
26. Give at least 3 factors causing protein denaturation.
27. Explain a method used for determination of proteins by spectrophotometry.
28. Enumerate amino acids containing -OH group in their side chain.
29. Enumerate amino acids containing sulfur in their side chain.
30. Enumerate amino acids containing an aromatic ring in their side chain.
31. Enumerate branched chain amino acids.
32. Enumerate acidic amino acids.
33. Enumerate basic amino acids.
34. Explain the term „essential amino acids“. Give their names.
35. What is the end product of protein degradation in a human body?
36. Localize synthesis of urea: in a human body and within cells.
37. How is urea cycle regulated?
38. What is the fate of urea?
39. Describe transport of ammonia in blood (its „nontoxic form“).
40. How can be glutamine metabolized in the kidney?
41. What amino acids can not be used for synthesis of glucose?