WGU C785 LATEST VERSION QUESTIONS AND ANSWERS
WITH STUDY GUIDE DETAILED AND VERIFIED FOR
GUARANTEED PASS, LATEST UPDATE 2025 GRADED A
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 Lovering, 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
WITH STUDY GUIDE DETAILED AND VERIFIED FOR
GUARANTEED PASS, LATEST UPDATE 2025 GRADED A
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 Lovering, 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
