Protein Study Guide PDF

Vet Prep- Cellular Biology and Homeostasis Study Guide AA AND PROTEINS 1. Describe the basic structure of a protein. 2. Describe the flow of informa on according to the central dogma of molecular biology. 3. L...

Vet Prep- Cellular Biology and Homeostasis Study Guide AA AND PROTEINS 1. Describe the basic structure of a protein. 2. Describe the flow of informa on according to the central dogma of molecular biology. 3. List the different func ons of membrane proteins. 4. Dis nguish between amino acids, oligopep des, polypep des and proteins. 5. Explain the basic, general structure of an amino acid. 6. Explain the pep de bond (condensa on reac on) its forma on and importance for protein synthesis. 7. Be familiar with the 20 standard amino acids, understand what are proteinogenic amino acids. 8. What are the four general groups of amino acids, what determines the biochemical behavior of an amino acid? 9. Understand the difference between amino acids with polar and those with nonpolar side chains. 10. Recall the importance of proline and his dine, and how their characteris cs depends on their structure. 11. Describe the uncharged polar AAs; which of them can form hydrogen bonds, what is special about cysteine? 12. Recall the AAs with acidic and basic side chains: which are proton donors, which are proton acceptors, how does this depend on the pH? 13. Understand the posi oning of the amino acids in a soluble protein or a plasma membrane protein (depending on polarity). 14. List important physiological compounds that are derived from modifica ons of single amino acids (amino acids deriva ves) and their basic func ons. 15. List and explain the physiologically important pep des and polypep des (as discussed in class) 16. Describe the diges on and absorp on of dietary proteins: a) Where diges on starts? b) List the diges ve enzymes, where they are produced and secreted. c) How are the products of diges on absorbed? d) What is the fate of dietary protein a er absorp on? 17. Nitrogen metabolism: what does it mean for nitrogen metabolism that AAs cannot be stored in the body, like lipids or carbohydrates? 18. How is nitrogen excreted from the body? 19. How can proteins be used for energy genera on in the body? 20. Briefly explain the gene c code (triplet code), what bases code for it, and how this is translated into the 20 proteinogenic amino acids. 21. Explain the gene c code characteris cs. 22. Name some differences between prokaryotes and eukaryotes regarding protein synthesis (transcrip on and transla on) 23. Briefly explain the importance of protein splicing and alterna ve splicing 24. Describe the process of protein biosynthesis: a. Ac va on, b. Ini a on, c. Elonga on d. Termina on e. what is the role of the tRNA? f. Where in the cell do the processes take place? 25. Explain the differences between cytosolic ribosomes and those bound to the rER. 26. Describe the fate of a newly synthesized protein. 27. Explain the importance of ER and Golgi apparatus for protein post-transla onal modifica ons. 28. Name the protein post-transla onal modifica ons and give some examples. 29. What is protein sor ng? 30. Explain some common muta ons deriving from altera ons in the nucleo de sequence, and their consequences. 31. What is sickle cell anemia, what is its cause and some effects for sufferers. 32. Understand the mains causes of protein muta on and effects. 33. Understand how protein muta ons can translate in posi ve changes. 34. Dis nguish and explain the primary, secondary, ter ary and quaternary structure of proteins. 35. List and explain the different types of secondary protein structures discussed, and what they mean for the proteins. 36. What bonds stabilize the alpha-helix? 37. Describe the characteris c of the beta-sheets and the beta-bends? 38. What is protein ter ary structure? a. What is a domain? b. What type of bonds can shape the ter ary structure? 39. Explain the quaternary protein structure and name some examples. 40. Describe the important chemical bonds par cipa ng in protein structure (primary, secondary, ter ary and quaternary). 41. Explain protein folding and why it is important for protein func on. 42. What are chaperones? a. What other names are used to describe them, b. What is their func on? 43. Describe protein denatura on and list some denaturing agents. 44. Understand the basic classifica ons of proteins: a) Structure b) Composi on c) Func on 45. What are the differences between simple and conjugated proteins, and what are the typical prosthe c groups of conjugated/complex proteins? Give some examples. 46. What are the main func ons of proteins in physiology?