WGU C785 FINAL EXAM QUIZ
GRADED A+
1. What is the basic structure of an amino acid? What do they
look like?
Ans: amino group (NH2 or NH3), carboxyl group (COO or
COOH), alpha carbon (C), and variable group
2. How do you identify the 3 different types of side chains:
non-polar/hydrophobic, polar, and charged?
Ans: Non-polar/hydrophobic - end with CH or "can't have" water.
Polar - end with OH, SH, or NH. Charged - end with a charge
3. what kinds of bonds do each of the 3 different types of
side chains make?
Ans: ionic, hydrophobic/non-polar, charged
4. What are the 4 levels of protein structure?
Ans: Primary - linear structure, Secondary
- Folded into helix or pleated sheet caused by hydrogen bonding,
tertiary -
3D structure caused by side chain interactions, quaternary - 1+
amino acid chains
combine = multiple subunits MUST have 1+ subunit
5. What environmental change breaks each type of bond?
Ans: hydrophobic – temperature change, ionic - salt or
decreased pH, hydrogen - temperature, change in pH, disulfide -
reducing agents
,6. what type of amino acid side chain leads to protein
aggregation?
Ans: hydrophobic bonds
7. How do environmental changes affect protein folding?
Ans: Extreme temp can cause hydrogen bonds to break apart =
malformation of protein folding
8. How do mutations affect protein structure?
Ans: Can cause structure to change. Protein loses form = loses
function. May form a different protein.
9. What is an electron?
Ans: Negatively charged atom on outer ring for bonding
10. What is energy?
Ans: Power derived from chemical interaction.
11. What are covalent bonds?
Ans: Chemical bond, atoms share 1+ valence electrons.
12. What is an ionic bond?
Ans: Bond between positive and negative
13. What is a hydrogen bond?
Ans: Weak bond between positive and negative
14. What is an amino?
Ans: Piece of amino acid, NH2 or NH3
15. what is a carboxyl?
,Ans: piece of amino acid, COO or COOH
16. What is hydrophobic?
Ans: Doesn't like water, end with CH
17. What is hydrophilic?
Ans: Water Lovering, end with OH, NH, or SH
18. what is disulfide bond?
Ans: Strongest bond between reduction agents, formed
between SH's.
19. What are zwitterions?
Ans: amino with positive and negative charges = overall
charge of zero
20. what is a polypeptide
Ans: Polymer of amino acids
21. What is dehydration synthesis?
Ans: Process of forming peptide bonds
22. What is hydrolysis?
Ans: adding water to destroy bonds
23. what is an alpha helix?
Ans: twisted secondary structure, formed by hydrogen bonds
24. What is a beta sheet?
Ans: folded second structure shape, formed by hydrogen bonds
, 25. What is denaturation?
Ans: loss of shape due to interruption of chemical bonds; occurs
via extreme salt, temp, pH
26. What is aggregation?
Ans: clumping of inner or outer cellular proteins caused by
misfolded proteins leading to diseases such as Alzheimer’s, ALS,
Parkinson's
27. How do enzymes catalyze reactions?
Ans: bind with substrates to decrease activation energy required
and decrease reaction rate
28. How do enzymes affect reaction rate and activation
energy?
Ans: decrease activation energy and decrease reaction rate
29. what are the 4 steps of the enzymatic cycle?
Ans: Enzyme recognizes substrate, substrate attracts the
enzyme; enzyme-substrate complex is formed; enzyme-
product complex formed; product is released, enzyme recycled
30. how do environmental changes affect enzymes?
Ans: High heat, pH change, high salt concentration, and reducing
agents can cause an enzyme to lose its form/lose function
31. What is a competitive inhibitor?
Ans: Mimics substrate and takes its place on the active binding
site
GRADED A+
1. What is the basic structure of an amino acid? What do they
look like?
Ans: amino group (NH2 or NH3), carboxyl group (COO or
COOH), alpha carbon (C), and variable group
2. How do you identify the 3 different types of side chains:
non-polar/hydrophobic, polar, and charged?
Ans: Non-polar/hydrophobic - end with CH or "can't have" water.
Polar - end with OH, SH, or NH. Charged - end with a charge
3. what kinds of bonds do each of the 3 different types of
side chains make?
Ans: ionic, hydrophobic/non-polar, charged
4. What are the 4 levels of protein structure?
Ans: Primary - linear structure, Secondary
- Folded into helix or pleated sheet caused by hydrogen bonding,
tertiary -
3D structure caused by side chain interactions, quaternary - 1+
amino acid chains
combine = multiple subunits MUST have 1+ subunit
5. What environmental change breaks each type of bond?
Ans: hydrophobic – temperature change, ionic - salt or
decreased pH, hydrogen - temperature, change in pH, disulfide -
reducing agents
,6. what type of amino acid side chain leads to protein
aggregation?
Ans: hydrophobic bonds
7. How do environmental changes affect protein folding?
Ans: Extreme temp can cause hydrogen bonds to break apart =
malformation of protein folding
8. How do mutations affect protein structure?
Ans: Can cause structure to change. Protein loses form = loses
function. May form a different protein.
9. What is an electron?
Ans: Negatively charged atom on outer ring for bonding
10. What is energy?
Ans: Power derived from chemical interaction.
11. What are covalent bonds?
Ans: Chemical bond, atoms share 1+ valence electrons.
12. What is an ionic bond?
Ans: Bond between positive and negative
13. What is a hydrogen bond?
Ans: Weak bond between positive and negative
14. What is an amino?
Ans: Piece of amino acid, NH2 or NH3
15. what is a carboxyl?
,Ans: piece of amino acid, COO or COOH
16. What is hydrophobic?
Ans: Doesn't like water, end with CH
17. What is hydrophilic?
Ans: Water Lovering, end with OH, NH, or SH
18. what is disulfide bond?
Ans: Strongest bond between reduction agents, formed
between SH's.
19. What are zwitterions?
Ans: amino with positive and negative charges = overall
charge of zero
20. what is a polypeptide
Ans: Polymer of amino acids
21. What is dehydration synthesis?
Ans: Process of forming peptide bonds
22. What is hydrolysis?
Ans: adding water to destroy bonds
23. what is an alpha helix?
Ans: twisted secondary structure, formed by hydrogen bonds
24. What is a beta sheet?
Ans: folded second structure shape, formed by hydrogen bonds
, 25. What is denaturation?
Ans: loss of shape due to interruption of chemical bonds; occurs
via extreme salt, temp, pH
26. What is aggregation?
Ans: clumping of inner or outer cellular proteins caused by
misfolded proteins leading to diseases such as Alzheimer’s, ALS,
Parkinson's
27. How do enzymes catalyze reactions?
Ans: bind with substrates to decrease activation energy required
and decrease reaction rate
28. How do enzymes affect reaction rate and activation
energy?
Ans: decrease activation energy and decrease reaction rate
29. what are the 4 steps of the enzymatic cycle?
Ans: Enzyme recognizes substrate, substrate attracts the
enzyme; enzyme-substrate complex is formed; enzyme-
product complex formed; product is released, enzyme recycled
30. how do environmental changes affect enzymes?
Ans: High heat, pH change, high salt concentration, and reducing
agents can cause an enzyme to lose its form/lose function
31. What is a competitive inhibitor?
Ans: Mimics substrate and takes its place on the active binding
site
