WGU C785 BIOCHEMISTRY FINAL EXAM 2026 WITH ALL
THE CORRECT ANSWERS | FROM QUESTION TO
PERFECTION| STUDY WITH CONFIDENCE!
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.
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, 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
APPHIA – Crafted with Care and Precision for Academic Excellence.
2
THE CORRECT ANSWERS | FROM QUESTION TO
PERFECTION| STUDY WITH CONFIDENCE!
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.
APPHIA – Crafted with Care and Precision for Academic Excellence.
1
, 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
APPHIA – Crafted with Care and Precision for Academic Excellence.
2
