WGU C785 Final Exam With All The Correct Answers
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
How do you identify the 3 different types of side chains: non-polar/hydrophobic, 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
what kinds of bonds do each of the 3 different types of side chains make?
ionic, hydrophobic/non-polar, charged
What are the 4 levels of protein structure?
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
What enviormental change breaks each type of bond?
hydrophobic - temperature change, ionic - salt or decreased pH, hydrogen -
temperature, change in pH, disulfide - reducing agents
what type of amino acid side chain leads to protein aggregration?
hydrophobic bonds
how do environmental changes affect protein folding?
Extreme temp can cause hydrogen bonds to break apart = malformation of protein
folding
how do mutations affect protein structure?
Can cause structure to change. Protein loses form = loses function. May form a different
protein.
What is an electron?
Negatively charged atom on outer ring for bonding
What is energy:
Power derived fro chemical interaction
what are covalent bonds?
chemical bond, atoms share 1+ valence electrons
what is an ionic bond?
bond between positive and negative
what is a hydrogen bond?
weak bond between positive and negative
with an amino?
piece of amino acid, NH2 or NH3
what is a carboyxl?
piece of amino acid, COO or COOH
What is hydrophobic?
Doesn't like water, end with CH
what is hydrophilic?
Water Lovering, end with OH, NH, or SH
what is disulfide bond?
strongest bond between reduction agents, formed between SH's.
, what are zwitterions?
amino with positive and negative charges = overall charge of zero
what is a polypeptide
polymer of amino acids
What is dehydration synthesis?
Process of forming peptide bonds
what is hydrolysis?
adding water to destroy bonds
what is an alpha helix?
twisted secondary structure, formed by hydrogen bonds
what is a beta sheet?
folded second structure shape, formed by hydrogen bonds
what is denaturation?
loss of shape duet o interruption of chemical bonds; occurs via extreme salt, temp, pH
what is aggregation?
clumping of inner or outer cellular proteins caused by misfolded proteins leading to
diseases such as Alzheimers, ALS, Parkinson's
how do enzymes catalyze reactions?
bind with substrates to decrease activation energy required and decrease reaction rate
how do enzymes affect reaction rate and activation energy?
decrease activation energy and decrease reaction rate
what are the 4 steps of the enzymatic cycle?
enzyme recognizes substrate, substrate attracts the enzyme; enzyme-substrate
complex is formed; enzyme-product complex formed; product is released, enzyme
recycled
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
what is a competitive inhibitor?
Mimics substrate and takes its place on the active binding site
what is a noncompetitive inhibitor?
Binds to allosteric site causing active site to change shape = preventing substrate from
binding with enzyme
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.
what is substrate?
the substance on which an enzyme acts
what is a product?
result of a reaction
what is an intermediate?
products produced in an enzyme pathway before final product
what is an active site?
location where substrate binds with enzyme
what is enzyme specificity?
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
How do you identify the 3 different types of side chains: non-polar/hydrophobic, 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
what kinds of bonds do each of the 3 different types of side chains make?
ionic, hydrophobic/non-polar, charged
What are the 4 levels of protein structure?
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
What enviormental change breaks each type of bond?
hydrophobic - temperature change, ionic - salt or decreased pH, hydrogen -
temperature, change in pH, disulfide - reducing agents
what type of amino acid side chain leads to protein aggregration?
hydrophobic bonds
how do environmental changes affect protein folding?
Extreme temp can cause hydrogen bonds to break apart = malformation of protein
folding
how do mutations affect protein structure?
Can cause structure to change. Protein loses form = loses function. May form a different
protein.
What is an electron?
Negatively charged atom on outer ring for bonding
What is energy:
Power derived fro chemical interaction
what are covalent bonds?
chemical bond, atoms share 1+ valence electrons
what is an ionic bond?
bond between positive and negative
what is a hydrogen bond?
weak bond between positive and negative
with an amino?
piece of amino acid, NH2 or NH3
what is a carboyxl?
piece of amino acid, COO or COOH
What is hydrophobic?
Doesn't like water, end with CH
what is hydrophilic?
Water Lovering, end with OH, NH, or SH
what is disulfide bond?
strongest bond between reduction agents, formed between SH's.
, what are zwitterions?
amino with positive and negative charges = overall charge of zero
what is a polypeptide
polymer of amino acids
What is dehydration synthesis?
Process of forming peptide bonds
what is hydrolysis?
adding water to destroy bonds
what is an alpha helix?
twisted secondary structure, formed by hydrogen bonds
what is a beta sheet?
folded second structure shape, formed by hydrogen bonds
what is denaturation?
loss of shape duet o interruption of chemical bonds; occurs via extreme salt, temp, pH
what is aggregation?
clumping of inner or outer cellular proteins caused by misfolded proteins leading to
diseases such as Alzheimers, ALS, Parkinson's
how do enzymes catalyze reactions?
bind with substrates to decrease activation energy required and decrease reaction rate
how do enzymes affect reaction rate and activation energy?
decrease activation energy and decrease reaction rate
what are the 4 steps of the enzymatic cycle?
enzyme recognizes substrate, substrate attracts the enzyme; enzyme-substrate
complex is formed; enzyme-product complex formed; product is released, enzyme
recycled
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
what is a competitive inhibitor?
Mimics substrate and takes its place on the active binding site
what is a noncompetitive inhibitor?
Binds to allosteric site causing active site to change shape = preventing substrate from
binding with enzyme
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.
what is substrate?
the substance on which an enzyme acts
what is a product?
result of a reaction
what is an intermediate?
products produced in an enzyme pathway before final product
what is an active site?
location where substrate binds with enzyme
what is enzyme specificity?
