WGU C785 FINAL EXAM 2024 EXAM AND STUDY GUIDE QUESTIONS
WITH DETAILED VERIFIED SOLUTIONS (100% CORRECT) FROM
PAST PAPER /A+ GRADE
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
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
what kinds of bonds do each of the 3 different types of side chains make? - (correct
answer) ionic, hydrophobic/non-polar, charged
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
What enviormental change breaks each type of bond? - (correct answer)
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? - (correct answer)
hydrophobic bonds
how do environmental changes affect protein folding? - (correct answer) Extreme
temp can cause hydrogen bonds to break apart = malformation of protein folding
how do mutations affect protein structure? - (correct answer) Can cause structure
to change. Protein loses form = loses function. May form a different protein.
What is an electron? - (correct answer) Negatively charged atom on outer ring for
bonding
What is energy: - (correct answer) Power derived fro chemical interaction
what are covalent bonds? - (correct answer) chemical bond, atoms share 1+
valence electrons
what is an ionic bond? - (correct answer) bond between positive and negative
what is a hydrogen bond? - (correct answer) weak bond between positive and
negative
,with an amino? - (correct answer) piece of amino acid, NH2 or NH3
what is a carboyxl? - (correct answer) piece of amino acid, COO or COOH
What is hydrophobic? - (correct answer) Doesn't like water, end with CH
what is hydrophilic? - (correct answer) Water loving, end with OH, NH, or SH
what is disulfide bond? - (correct answer) strongest bond between reduction
agents, formed between SH's.
what are zwitterions? - (correct answer) amino with positive and negative charges
= overall charge of zero
what is a polypeptide - (correct answer) polymer of amino acids
What is dehydration synthesis? - (correct answer) Process of forming peptide
bonds
what is hydrolysis? - (correct answer) adding water to destroy bonds
what is an alpha helix? - (correct answer) twisted secondary structure, formed by
hydrogen bonds
what is a beta sheet? - (correct answer) folded second structure shape, formed by
hydrogen bonds
what is denaturation? - (correct answer) loss of shape duet o interruption of
chemical bonds; occurs via extreme salt, temp, pH
what is aggregation? - (correct answer) 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? - (correct answer) bind with substrates to
decrease activation energy required and decrease reaction rate
how do enzymes affect reaction rate and activation energy? - (correct answer)
decrease activation energy and decrease reaction rate
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
, 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
what is a competitive inhibitor? - (correct answer) Mimics substrate and takes its
place on the active binding site
what is a noncompetitive inhibitor? - (correct answer) 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. -
(correct answer) Inhibitor would cause a build up for product B, decrease product C.
Enzyme 3 and product D would not be created.
what is substrate? - (correct answer) the substance on which an enzyme acts
what is a product? - (correct answer) result of a reaction
what is an intermediate? - (correct answer) products produced in an enzyme
pathway before final product
what is an active site? - (correct answer) location where substrate binds with
enzyme
what is enzyme specificity? - (correct answer) Enzymes bind with certain substrate
or type of substrate to create a certain reaction
what is induced fit? - (correct answer) Enzyme changes shape in enzyme-
substrate complex to facilitate formation of enzyme-product complex
what is kinase? - (correct answer) Enzyme, adds phosphate group via
phosphorlation
what is phosphatase? - (correct answer) enzyme, removes phosphate group via
dephosphorylation
with is an allosteric site? - (correct answer) secondary site on an enzyme an
inhibitor binds to via non-competitive inhibition
what is competitive inhibition? - (correct answer) enzyme substrate and inhibitor
complex compete to bind with enzyme's active site. no product formed when inhibitor
binds with enzyme.
WITH DETAILED VERIFIED SOLUTIONS (100% CORRECT) FROM
PAST PAPER /A+ GRADE
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
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
what kinds of bonds do each of the 3 different types of side chains make? - (correct
answer) ionic, hydrophobic/non-polar, charged
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
What enviormental change breaks each type of bond? - (correct answer)
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? - (correct answer)
hydrophobic bonds
how do environmental changes affect protein folding? - (correct answer) Extreme
temp can cause hydrogen bonds to break apart = malformation of protein folding
how do mutations affect protein structure? - (correct answer) Can cause structure
to change. Protein loses form = loses function. May form a different protein.
What is an electron? - (correct answer) Negatively charged atom on outer ring for
bonding
What is energy: - (correct answer) Power derived fro chemical interaction
what are covalent bonds? - (correct answer) chemical bond, atoms share 1+
valence electrons
what is an ionic bond? - (correct answer) bond between positive and negative
what is a hydrogen bond? - (correct answer) weak bond between positive and
negative
,with an amino? - (correct answer) piece of amino acid, NH2 or NH3
what is a carboyxl? - (correct answer) piece of amino acid, COO or COOH
What is hydrophobic? - (correct answer) Doesn't like water, end with CH
what is hydrophilic? - (correct answer) Water loving, end with OH, NH, or SH
what is disulfide bond? - (correct answer) strongest bond between reduction
agents, formed between SH's.
what are zwitterions? - (correct answer) amino with positive and negative charges
= overall charge of zero
what is a polypeptide - (correct answer) polymer of amino acids
What is dehydration synthesis? - (correct answer) Process of forming peptide
bonds
what is hydrolysis? - (correct answer) adding water to destroy bonds
what is an alpha helix? - (correct answer) twisted secondary structure, formed by
hydrogen bonds
what is a beta sheet? - (correct answer) folded second structure shape, formed by
hydrogen bonds
what is denaturation? - (correct answer) loss of shape duet o interruption of
chemical bonds; occurs via extreme salt, temp, pH
what is aggregation? - (correct answer) 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? - (correct answer) bind with substrates to
decrease activation energy required and decrease reaction rate
how do enzymes affect reaction rate and activation energy? - (correct answer)
decrease activation energy and decrease reaction rate
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
, 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
what is a competitive inhibitor? - (correct answer) Mimics substrate and takes its
place on the active binding site
what is a noncompetitive inhibitor? - (correct answer) 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. -
(correct answer) Inhibitor would cause a build up for product B, decrease product C.
Enzyme 3 and product D would not be created.
what is substrate? - (correct answer) the substance on which an enzyme acts
what is a product? - (correct answer) result of a reaction
what is an intermediate? - (correct answer) products produced in an enzyme
pathway before final product
what is an active site? - (correct answer) location where substrate binds with
enzyme
what is enzyme specificity? - (correct answer) Enzymes bind with certain substrate
or type of substrate to create a certain reaction
what is induced fit? - (correct answer) Enzyme changes shape in enzyme-
substrate complex to facilitate formation of enzyme-product complex
what is kinase? - (correct answer) Enzyme, adds phosphate group via
phosphorlation
what is phosphatase? - (correct answer) enzyme, removes phosphate group via
dephosphorylation
with is an allosteric site? - (correct answer) secondary site on an enzyme an
inhibitor binds to via non-competitive inhibition
what is competitive inhibition? - (correct answer) enzyme substrate and inhibitor
complex compete to bind with enzyme's active site. no product formed when inhibitor
binds with enzyme.
