WGU C785
FINAL
EXAM
QUIZ
GRADED
A+
, WGU C785 FINAL
EXAM QUIZ
GRADED A+
1. What is the basic structure of an amino acid? What do they look like?:
- 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/hy-
drophobic, polar, and charged?: 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?: ionic, hydrophobic/non-polar, charged
4. What are the 4 levels of protein structure?: Primary - linear structure,
Sec-ondary - 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 enviormental change breaks each type of bond?: hydrophobic -
tem-perature 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 aggregration?:
hy- drophobic bonds
7. how do environmental changes affect protein folding?: Extreme
temp can cause hydrogen bonds to break apart = malformation of
,protein folding
8. how do mutations affect protein structure?: Can cause structure
to change. Protein loses form = loses function. May form a
different protein.
9.What is an electron?: Negatively charged atom on outer ring for
bonding
10.What is energy:: Power derived fro chemical interaction
11.what are covalent bonds?: chemical bond, atoms share 1+
valence electrons
12.what is an ionic bond?: bond between positive and negative
13.what is a hydrogen bond?: weak bond between positive and negative
14.with an amino?: piece of amino acid, NH2 or NH3
15.what is a carboyxl?: piece of amino acid, COO or COOH
16.What is hydrophobic?: Doesn't like water, end with CH
17.what is hydrophilic?: Water Lovering, end with OH, NH, or SH
18.what is disulfide bond?: strongest bond between reduction
agents, formed between SH's.
19.what are zwitterions?: amino with positive and negative
charges = overall charge of zero
20.what is a polypeptide: polymer of amino acids
21.What is dehydration synthesis?: Process of forming peptide bonds
22.what is hydrolysis?: adding water to destroy bonds
23.what is an alpha helix?: twisted secondary structure,
formed by hydrogen bonds
24.what is a beta sheet?: folded second structure shape,
formed by hydrogen bonds
25.what is denaturation?: loss of shape duet o interruption of
chemical bonds; occurs via extreme salt, temp, pH
26.what is aggregation?: clumping of inner or outer cellular proteins
caused by misfolded proteins leading to diseases such as Alzheimers,
ALS, Parkinson's
27.how do enzymes catalyze reactions?: bind with substrates
, to decrease activation energy required and decrease
reaction rate
28.how do enzymes affect reaction rate and activation energy?:
decrease activation energy and decrease reaction rate
29.what are the 4 steps of the enzymatic cycle?: enzyme recognizes
sub-strate, substrate attracts the enzyme; enzyme-substrate
complex is formed; en- zyme-product complex formed; product is
released, enzyme recycled
30.how do environmental changes affect enzymes?: 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?: Mimics substrate and takes its
place on the active binding site
32.what is a noncompetitive inhibitor?: 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 inhibited.: Inhibitor would cause a build up for
product B, decrease product C. Enzyme 3 and product D would not be
created.
34.what is substrate?: the substance on which an enzyme acts
35.what is a product?: result of a reaction
FINAL
EXAM
QUIZ
GRADED
A+
, WGU C785 FINAL
EXAM QUIZ
GRADED A+
1. What is the basic structure of an amino acid? What do they look like?:
- 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/hy-
drophobic, polar, and charged?: 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?: ionic, hydrophobic/non-polar, charged
4. What are the 4 levels of protein structure?: Primary - linear structure,
Sec-ondary - 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 enviormental change breaks each type of bond?: hydrophobic -
tem-perature 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 aggregration?:
hy- drophobic bonds
7. how do environmental changes affect protein folding?: Extreme
temp can cause hydrogen bonds to break apart = malformation of
,protein folding
8. how do mutations affect protein structure?: Can cause structure
to change. Protein loses form = loses function. May form a
different protein.
9.What is an electron?: Negatively charged atom on outer ring for
bonding
10.What is energy:: Power derived fro chemical interaction
11.what are covalent bonds?: chemical bond, atoms share 1+
valence electrons
12.what is an ionic bond?: bond between positive and negative
13.what is a hydrogen bond?: weak bond between positive and negative
14.with an amino?: piece of amino acid, NH2 or NH3
15.what is a carboyxl?: piece of amino acid, COO or COOH
16.What is hydrophobic?: Doesn't like water, end with CH
17.what is hydrophilic?: Water Lovering, end with OH, NH, or SH
18.what is disulfide bond?: strongest bond between reduction
agents, formed between SH's.
19.what are zwitterions?: amino with positive and negative
charges = overall charge of zero
20.what is a polypeptide: polymer of amino acids
21.What is dehydration synthesis?: Process of forming peptide bonds
22.what is hydrolysis?: adding water to destroy bonds
23.what is an alpha helix?: twisted secondary structure,
formed by hydrogen bonds
24.what is a beta sheet?: folded second structure shape,
formed by hydrogen bonds
25.what is denaturation?: loss of shape duet o interruption of
chemical bonds; occurs via extreme salt, temp, pH
26.what is aggregation?: clumping of inner or outer cellular proteins
caused by misfolded proteins leading to diseases such as Alzheimers,
ALS, Parkinson's
27.how do enzymes catalyze reactions?: bind with substrates
, to decrease activation energy required and decrease
reaction rate
28.how do enzymes affect reaction rate and activation energy?:
decrease activation energy and decrease reaction rate
29.what are the 4 steps of the enzymatic cycle?: enzyme recognizes
sub-strate, substrate attracts the enzyme; enzyme-substrate
complex is formed; en- zyme-product complex formed; product is
released, enzyme recycled
30.how do environmental changes affect enzymes?: 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?: Mimics substrate and takes its
place on the active binding site
32.what is a noncompetitive inhibitor?: 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 inhibited.: Inhibitor would cause a build up for
product B, decrease product C. Enzyme 3 and product D would not be
created.
34.what is substrate?: the substance on which an enzyme acts
35.what is a product?: result of a reaction
