WGU C785 Final Exam 2025 With All The Correct
Answers
/. What is the basic structure of an amino acid? What do they look like? - 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? - 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? - Answer-
✅ionic, hydrophobic/non-polar, charged
/.What are the 4 levels of protein structure? - 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? - 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? - Answer-
✅hydrophobic bonds
/.how do environmental changes affect protein folding? - Answer-✅Extreme temp can
cause hydrogen bonds to break apart = malformation of protein folding
/.how do mutations affect protein structure? - Answer-✅Can cause structure to change.
Protein loses form = loses function. May form a different protein.
/.What is an electron? - Answer-✅Negatively charged atom on outer ring for bonding
/.What is energy: - Answer-✅Power derived fro chemical interaction
/.what are covalent bonds? - Answer-✅chemical bond, atoms share 1+ valence
electrons
/.what is an ionic bond? - Answer-✅bond between positive and negative
,/.what is a hydrogen bond? - Answer-✅weak bond between positive and negative
/.with an amino? - Answer-✅piece of amino acid, NH2 or NH3
/.what is a carboyxl? - Answer-✅piece of amino acid, COO or COOH
/.What is hydrophobic? - Answer-✅Doesn't like water, end with CH
/.what is hydrophilic? - Answer-✅Water Lovering, end with OH, NH, or SH
/.what is disulfide bond? - Answer-✅strongest bond between reduction agents, formed
between SH's.
/.what are zwitterions? - Answer-✅amino with positive and negative charges = overall
charge of zero
/.what is a polypeptide - Answer-✅polymer of amino acids
/.What is dehydration synthesis? - Answer-✅Process of forming peptide bonds
/.what is hydrolysis? - Answer-✅adding water to destroy bonds
/.what is an alpha helix? - Answer-✅twisted secondary structure, formed by hydrogen
bonds
/.what is a beta sheet? - Answer-✅folded second structure shape, formed by hydrogen
bonds
/.what is denaturation? - Answer-✅loss of shape duet o interruption of chemical bonds;
occurs via extreme salt, temp, pH
/.what is aggregation? - 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? - Answer-✅bind with substrates to decrease
activation energy required and decrease reaction rate
/.how do enzymes affect reaction rate and activation energy? - Answer-✅decrease
activation energy and decrease reaction rate
/.what are the 4 steps of the enzymatic cycle? - 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? - 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? - Answer-✅Mimics substrate and takes its place on the
active binding site
/.what is a noncompetitive inhibitor? - 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. - 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? - Answer-✅the substance on which an enzyme acts
/.what is a product? - Answer-✅result of a reaction
/.what is an intermediate? - Answer-✅products produced in an enzyme pathway before
final product
/.what is an active site? - Answer-✅location where substrate binds with enzyme
/.what is enzyme specificity? - Answer-✅Enzymes bind with certain substrate or type of
substrate to create a certain reaction
/.what is induced fit? - Answer-✅Enzyme changes shape in enzyme-substrate complex
to facilitate formation of enzyme-product complex
/.what is kinase? - Answer-✅Enzyme, adds phosphate group via phosphorlation
/.what is phosphatase? - Answer-✅enzyme, removes phosphate group via
dephosphorylation
/.with is an allosteric site? - Answer-✅secondary site on an enzyme an inhibitor binds to
via non-competitive inhibition
/.what is competitive inhibition? - Answer-✅enzyme substrate and inhibitor complex
compete to bind with enzyme's active site. no product formed when inhibitor binds with
enzyme.
Answers
/. What is the basic structure of an amino acid? What do they look like? - 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? - 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? - Answer-
✅ionic, hydrophobic/non-polar, charged
/.What are the 4 levels of protein structure? - 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? - 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? - Answer-
✅hydrophobic bonds
/.how do environmental changes affect protein folding? - Answer-✅Extreme temp can
cause hydrogen bonds to break apart = malformation of protein folding
/.how do mutations affect protein structure? - Answer-✅Can cause structure to change.
Protein loses form = loses function. May form a different protein.
/.What is an electron? - Answer-✅Negatively charged atom on outer ring for bonding
/.What is energy: - Answer-✅Power derived fro chemical interaction
/.what are covalent bonds? - Answer-✅chemical bond, atoms share 1+ valence
electrons
/.what is an ionic bond? - Answer-✅bond between positive and negative
,/.what is a hydrogen bond? - Answer-✅weak bond between positive and negative
/.with an amino? - Answer-✅piece of amino acid, NH2 or NH3
/.what is a carboyxl? - Answer-✅piece of amino acid, COO or COOH
/.What is hydrophobic? - Answer-✅Doesn't like water, end with CH
/.what is hydrophilic? - Answer-✅Water Lovering, end with OH, NH, or SH
/.what is disulfide bond? - Answer-✅strongest bond between reduction agents, formed
between SH's.
/.what are zwitterions? - Answer-✅amino with positive and negative charges = overall
charge of zero
/.what is a polypeptide - Answer-✅polymer of amino acids
/.What is dehydration synthesis? - Answer-✅Process of forming peptide bonds
/.what is hydrolysis? - Answer-✅adding water to destroy bonds
/.what is an alpha helix? - Answer-✅twisted secondary structure, formed by hydrogen
bonds
/.what is a beta sheet? - Answer-✅folded second structure shape, formed by hydrogen
bonds
/.what is denaturation? - Answer-✅loss of shape duet o interruption of chemical bonds;
occurs via extreme salt, temp, pH
/.what is aggregation? - 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? - Answer-✅bind with substrates to decrease
activation energy required and decrease reaction rate
/.how do enzymes affect reaction rate and activation energy? - Answer-✅decrease
activation energy and decrease reaction rate
/.what are the 4 steps of the enzymatic cycle? - 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? - 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? - Answer-✅Mimics substrate and takes its place on the
active binding site
/.what is a noncompetitive inhibitor? - 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. - 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? - Answer-✅the substance on which an enzyme acts
/.what is a product? - Answer-✅result of a reaction
/.what is an intermediate? - Answer-✅products produced in an enzyme pathway before
final product
/.what is an active site? - Answer-✅location where substrate binds with enzyme
/.what is enzyme specificity? - Answer-✅Enzymes bind with certain substrate or type of
substrate to create a certain reaction
/.what is induced fit? - Answer-✅Enzyme changes shape in enzyme-substrate complex
to facilitate formation of enzyme-product complex
/.what is kinase? - Answer-✅Enzyme, adds phosphate group via phosphorlation
/.what is phosphatase? - Answer-✅enzyme, removes phosphate group via
dephosphorylation
/.with is an allosteric site? - Answer-✅secondary site on an enzyme an inhibitor binds to
via non-competitive inhibition
/.what is competitive inhibition? - Answer-✅enzyme substrate and inhibitor complex
compete to bind with enzyme's active site. no product formed when inhibitor binds with
enzyme.
