WGU C785 Biochemistry Unit Exam Questions
with Answers
1. What is the basic structure of an amino acid? What do they look like? -
Correct answer 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? - Correct answer
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? -
Correct answer ionic, hydrophobic/non-polar, charged
4. What are the 4 levels of protein structure? - Correct answer 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? - Correct answer
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? - Correct
answer hydrophobic bonds
[Date]
1
,7. how do environmental changes affect protein folding? - Correct answer
Extreme temp can cause hydrogen bonds to break apart = malformation of
protein folding
8. how do mutations affect protein structure? - Correct answer Can cause
structure to change. Protein loses form = loses function. May form a
different protein.
9. What is an electron? - Correct answer Negatively charged atom on outer
ring for bonding
10.What is energy: - Correct answer Power derived from chemical interaction
11.what are covalent bonds? - Correct answer chemical bond, atoms share 1+
valence electrons
12.what is an ionic bond? - Correct answer bond between positive and
negative
13.what is a hydrogen bond? - Correct answer weak bond between positive
and negative
14.with an amino? - Correct answer piece of amino acid, NH2 or NH3
15.What is a carboxyl? - Correct answer piece of amino acid, COO or COOH
16.What is hydrophobic? - Correct answer Doesn't like water, end with CH
[Date]
2
,17.what is hydrophilic? - Correct answer Water Levering, end with OH, NH, or
SH
18.what is disulfide bond? - Correct answer strongest bond between reduction
agents, formed between SH's.
19.what are zwitterions? - Correct answer amino with positive and negative
charges = overall charge of zero
20.what is a polypeptide - Correct answer polymer of amino acids
21.What is dehydration synthesis? - Correct answer Process of forming peptide
bonds
22.what is hydrolysis? - Correct answer adding water to destroy bonds
23.what is an alpha helix? - Correct answer twisted secondary structure,
formed by hydrogen bonds
24.what is a beta sheet? - Correct answer folded second structure shape,
formed by hydrogen bonds
25.what is denaturation? - Correct answer loss of shape due to interruption of
chemical bonds; occurs via extreme salt, temp, pH
[Date]
3
, 26.what is aggregation? - Correct answer 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? - Correct answer bind with substrates
to decrease activation energy required and decrease reaction rate
28.how do enzymes affect reaction rate and activation energy? - Correct
answer decrease activation energy and decrease reaction rate
29.what are the 4 steps of the enzymatic cycle? - Correct answer 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? - Correct answer 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? - Correct answer Mimics substrate and
takes its place on the active binding site
32.what is a noncompetitive inhibitor? - Correct answer Binds to allosteric site
causing active site to change shape = preventing substrate from binding
with enzyme
33.what molecules increase/build up or decrease given a specific inhibitor? A -
> (enzyme 1) -> B -> (enzyme 2) -> C -> (enzyme 3) -> D. Pretend Enzyme 2 is
[Date]
4
with Answers
1. What is the basic structure of an amino acid? What do they look like? -
Correct answer 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? - Correct answer
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? -
Correct answer ionic, hydrophobic/non-polar, charged
4. What are the 4 levels of protein structure? - Correct answer 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? - Correct answer
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? - Correct
answer hydrophobic bonds
[Date]
1
,7. how do environmental changes affect protein folding? - Correct answer
Extreme temp can cause hydrogen bonds to break apart = malformation of
protein folding
8. how do mutations affect protein structure? - Correct answer Can cause
structure to change. Protein loses form = loses function. May form a
different protein.
9. What is an electron? - Correct answer Negatively charged atom on outer
ring for bonding
10.What is energy: - Correct answer Power derived from chemical interaction
11.what are covalent bonds? - Correct answer chemical bond, atoms share 1+
valence electrons
12.what is an ionic bond? - Correct answer bond between positive and
negative
13.what is a hydrogen bond? - Correct answer weak bond between positive
and negative
14.with an amino? - Correct answer piece of amino acid, NH2 or NH3
15.What is a carboxyl? - Correct answer piece of amino acid, COO or COOH
16.What is hydrophobic? - Correct answer Doesn't like water, end with CH
[Date]
2
,17.what is hydrophilic? - Correct answer Water Levering, end with OH, NH, or
SH
18.what is disulfide bond? - Correct answer strongest bond between reduction
agents, formed between SH's.
19.what are zwitterions? - Correct answer amino with positive and negative
charges = overall charge of zero
20.what is a polypeptide - Correct answer polymer of amino acids
21.What is dehydration synthesis? - Correct answer Process of forming peptide
bonds
22.what is hydrolysis? - Correct answer adding water to destroy bonds
23.what is an alpha helix? - Correct answer twisted secondary structure,
formed by hydrogen bonds
24.what is a beta sheet? - Correct answer folded second structure shape,
formed by hydrogen bonds
25.what is denaturation? - Correct answer loss of shape due to interruption of
chemical bonds; occurs via extreme salt, temp, pH
[Date]
3
, 26.what is aggregation? - Correct answer 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? - Correct answer bind with substrates
to decrease activation energy required and decrease reaction rate
28.how do enzymes affect reaction rate and activation energy? - Correct
answer decrease activation energy and decrease reaction rate
29.what are the 4 steps of the enzymatic cycle? - Correct answer 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? - Correct answer 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? - Correct answer Mimics substrate and
takes its place on the active binding site
32.what is a noncompetitive inhibitor? - Correct answer Binds to allosteric site
causing active site to change shape = preventing substrate from binding
with enzyme
33.what molecules increase/build up or decrease given a specific inhibitor? A -
> (enzyme 1) -> B -> (enzyme 2) -> C -> (enzyme 3) -> D. Pretend Enzyme 2 is
[Date]
4
