BIOCHEMISTRY QUESTIONS
GENERAL INFORMATION ABOUT ORGANIC MOLECULES
1. What are two characteristics of organic molecules?
2. Name the four kinds of organic molecules.
3. What is a functional group? Why are functional groups important in the study of biochemistry?
4. Why is direction important in the building of organic molecules?
5. The reactions that occur in the cell require what two things?
6. What are the 5 categories of reactions that occur within a cell?
7. What happens in a condensation reaction? What is another name for a condensation reaction?
8. What happens in a hydrolysis reaction? What is another name for a cleavage reaction?
9. What is the difference between a monomer and a polymer?
10. All organic molecules are made by putting _____ molecules ______ to make a _____ molecule.
11. Monomers are bonded together to form polymers by a reaction called ______ _____, or __________.
12. Polymers are broken down into monomers by a reaction called ________.
13. Create a table with 3 columns. The headings for the columns should be “Monomer”, “Polymer” and
“Name of Bond”. Fill it in, except leave the “Name of Bond” column blank. Include both names
for carbohydrates and lipids.
14. What does a condensation reaction do with 2 monomers?
15. What kind of bond is formed between two monomers during a condensation reaction?
16. What is a residue? When is it formed? How is it formed?
17. Does a dehydration synthesis reaction release or require energy?
18. Define polymerization.
19. What does a hydrolysis reaction do to a polymer?
20. A hydrolysis reaction requires the ______ of a _____ molecule.
21. Why does a hydrolysis reaction require the addition of a water molecule?
22. Does a hydrolysis reaction release or require energy?
23. What are 4 important facts about carbon that explain why it has a central role in the formation of
organic molecules?
24. What is a molecule’s backbone? How is a molecule’s backbone determined?
25. _______________ are compounds that consist of only carbon and hydrogen.
CARBOHDYRATES
1. Name the 3 kinds of carbohydrates.
2. Which kind of carbohydrate is the simple sugars?
3. Which kind of carbohydrate is considered ready energy for living organism?
4. Name 5 examples of monosaccharides. What do you notice about the last three letters in each word?
5. What is the general formula for monosaccharides?
6. Which functional group does a monosaccharide ALWAYS contain?
7. For its second functional group, a monosaccharide contains either a __________ or a _____________.
8. If a monosaccharide contains an aldehyde group, it is called a(n) _________.
9. If a monosaccharide contains a ketone group, it is called a(n) ________.
10. If a monosaccharide contains 3 carbons, it is called a ______________.
11. If a monosaccharide contains 4 carbons, it is called a _________________.
12. If a monosaccharide contains 5 carbons, it is called a __________.
13. If a monosaccharide contains 6 carbons, it is called a ____________.
14. Monosaccharides have a ____ ______ form and a ___ form
15. What is the molecular formula for glucose?
16. Besides hydroxyl, glucose contains the functional group _________, so it is called a(n) ____________.
17. Glucose contains _________ carbons, so it is called a _________.
18. Glucose functions as an ______________ source. During what cellular process does this occur?
19. What is the function of ribose and deoxyribose?
20. How many carbons do ribose and deoxyribose have?
21. A dimer of monosaccharides is a _____________. Why is it called a dimer?
22. How are disaccharides formed? What type of bond is formed?
23. The covalent bond between 2 monomers in a disaccharide or a polysaccharide is called a _____ _____.
Add this name to your chart from #13 in the first section of questions.
24. What is the function of disaccharides?
25. When energy is needed in a cell, what happens to the disaccharide?
26. ________ are long chains of monosaccharides, with each two monosaccharides being bonded together
by a ___________ reaction.
27. What are the two functions of polysaccharides?
28. Storage polysaccharides are made (________ reaction) when there is a _____ of sugar in the organism.
29. Storage polysaccharides are broken down (_______ reaction) when there is a ______ of sugar in the
organism.
30. Name the two kinds of storage polysaccharides. Which one is found in plant cells? Which one is found
in animal cells?
31. Where is glycogen stored?
32. When glucose is needed by an animal’s body, what does the body do?
33. What are two structural polysaccharides?
34. Where is cellulose found? What is its function?
35. What characteristic of cellulose causes it to make a plant rigid?
36. What type of molecule is chitin, and where is it found?
37. What is meant by “directionality”? Why is it important?
LIPIDS
1. What are 4 functions of lipids?
2. Structural lipids serve as components of ______, where they separate ______ compartments.
3. What are the “monomers” of fatty acids? Why is “monomers” in quotation marks?
4. Describe a fatty acid.
5. Fatty acids are either _____ or _____, depending upon whether their chain is filled with H atoms.
6. Saturated fatty acids have a hydrocarbon chain that is ______ with H atoms.
7. Saturated fatty acids have all ______ bonds.
8. Saturated fatty acids are common in ________.
9. Unsaturated fatty acids have hydrocarbon chains that are _____ ____ with H atoms.
10. Unsaturated fatty acids have ______ or ______ bonds.
11. Unsaturated fatty acids are common in _______.
12. In fatty acids, one end is __________ (water loving) and the other end is _______ (water hating)
13. The hydrophilic end of a fatty acid will dissolve in ______ because it is _______.
14. The hydrophilic end of a fatty acid is the _________ group.
15. The hydrophobic end of a fatty acid will dissolve in ____ solutions because it is ___.
16. The hydrophobic end of a fatty acid is the ____________ chain.
17. Name the five types of lipids (polymers of fatty acids).
18. The monomers of lipids are held together by what type of linkage? Add this name to your chart from
#13 in the first section of questions.
19. Which lipid is also called the fats? What were the fats formerly known as?
20. How are fats formed (what molecules are bonded together to form a fat?) What reaction occurs? What
kind of bonds are formed?
21. What is the function of a tricylglycerol (fat) molecule?
22. How are phospholipids formed (what molecules are bonded together to form a phospholipid?) What
reaction occurs? What kind of bonds are formed?
23. The polar (___________) head of a phospholipid is made of what two things?
24. The nonpolar (___________) tail of a phospholipid is made of what two things?
25. What is the function of phospholipids?
26. Draw a simple picture to illustrate how phospholipids form the structural basis of a cell membrane.
27. A cell membrane is ______ layers of phospholipids, with the _____ touching each other.
28. How are glycolipids formed (what molecules are bonded together to form a glycolipid?) What reaction
occurs? What kind of bonds are formed?
29. Glycolipids are important in the structure of ________ __________.
30. Describe the structure of a steroid.
31. Name the two types of steroids.
32. What is the function of cholesterol?
33. What is a hormone?
PROTEINS
1. Name the 5 parts of an amino acid. Which part of the amino acid is at the center (all the other parts are
attached to it)?
2. What makes one amino acid different from another amino acid?
3. During the condensation reaction that forms a polypeptide, the _______ group of amino acid reacts with
the____________ of the other amino acid.
4. In the formation of polypeptides, every two amino acids are bonded together by a_______ _____bond.
Add this name to your chart from #13 in the first section of questions.
5. What type of reaction bonds two amino acids together?
6. What are the 4 levels of protein structure?
7. Describe primary structure. What word describes the primary structure of a protein?
8. Why is it important for the primary structure of a protein to be correct?
9. What type of bond causes a protein’s secondary structure? What are the two possible forms for
secondary structure?
10. Describe the difference between the alpha helix and the beta-pleated sheet.
11. Describe the tertiary structure of proteins.
12. What 4 types of interactions between R groups influence a protein's tertiary structure?
13. What are disulfide bonds?
14. What causes hydrophobic interactions in tertiary structure?
15. Describe the quaternary structure of proteins.
16. Do all proteins have a quaternary structure? Explain.
17. Proteins have a “direction”, which means they have a _________ end and a __________ end. Why is it
important for a protein’s direction to be correct?
18. What are two types of fibrous structural proteins? What are their functions?
19. What is the function of globular structural proteins?
20. Hemoglobin is a __________ protein composed of ____ polypeptides chains around a "_____"
(______ containing) molecule.
21. What is the function of hemoglobin? Where is it found?
22. Why would it be beneficial to have more than one kind of hemoglobin?
23. What amino acid issue causes sickle cell anemia? Give a general answer and a specific answer.
24. Sickle cell anemia does what to the red blood cells? Why is this harmful to the person?
25. What type of protein is insulin? What is its function?
26. What is the cue in the body that causes the pancreas to release insulin?
27. Enzymes are protein molecules that act as __________ (they _____ ____ reactions
28. A catalyst regulates the ____ of a ______ reaction and itself remains ________.
29. What does denatured mean?
30. What can cause an enzyme to be denatured?
31. If a protein is only partially denatured, what occurs if it is returned to its normal surroundings?
32. Why is it harmful to a person if their enzymes are denatured?
33. Explain why enzymes are important in metabolism – why are they needed in order for chemical
reactions to occur.
34. Define energy of activation.
35. Enzymes act as a catalyst because they do what? How do they do that?
36. Define substrate.
37. What is the relationship between an active site and an enzyme?
38. How is an active site formed?
39. How does the active site’s 3-dimensional shape and characteristics compare to that of the substrate?
40. Explain in detail the induced-fit hypothesis. Be thorough.
41. Are enzymes globular proteins or fibrous proteins?
42. Is an enzyme permanently altered when it catalyzes a reaction? What does an enzyme do once it is
finished catalyzing a reaction?
43. Because of enzymes, cells can carry out chemical reactions at a great _______ and at comparatively
____ temperatures.
44. Enzymes are typically effective in ____ amounts.
45. Enzymes catalyze a ______ chemical reaction.
46. What is the role of a cofactor and a coenzyme?
47. What is the purpose of an allosteric interaction?
48. If an enzyme interacts allosterically, then it has 2 binding sites; the active site and a site where the
________ __________ fits.
49. What effect does an allosteric effector have an enzyme that it binds to?
50. Why is it important to regulate enzyme activity?
51. Name the 2 types of enzyme inhibition.
52. In competitive inhibition, the inhibitory molecule binds to the enzyme at what site? What effect does
this have on the enzyme?
53. In competitive inhibition, why must the inhibitory molecule resemble the substrate?
54. In noncompetitive inhibition, the inhibitory molecule binds to the enzyme in what site?
55. Explain feedback inhibition. Draw a simple sketch of feedback inhibition.
56. Briefly list 5 ways cells regulate the rates of its reactions.
57. Explain how changes in temperature affect enzyme activity.
58. Explain how changes in pH affect enzyme activity.