WGU C785 BIOCHEMISTRY Unit Exam
Questions & Answers Latest
2026/2027 with complete solution
What is the basic structure of an amino amino group (NH2 or NH3), carboxyl group (COO or COOH),
acid? What do they look like? alpha carbon (C), and variable group
How do you identify the 3 different types of Non-polar/hydrophobic - end with CH or "can't have" water.
side chains: non-polar/hydrophobic, polar, Polar - end with OH, SH, or NH. Charged - end with a charge
and charged?
what kinds of bonds do each of the 3 ionic, hydrophobic/non-polar, charged
different types of side chains make?
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 hydrophobic - temperature change, ionic - salt or decreased
type of bond? pH, hydrogen - temperature, change in pH, disulfide -
reducing agents
,what type of amino acid side chain leads to hydrophobic bonds
protein aggregration?
how do environmental changes affect Extreme temp can cause hydrogen bonds to break apart =
protein folding? 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 decrease activation energy and decrease reaction rate
activation energy?
what are the 4 steps of the enzymatic enzyme recognizes substrate, substrate attracts the enzyme;
cycle? enzyme-substrate complex is formed; enzyme-product
complex formed; product is released, enzyme recycled
how do environmental changes affect High heat, pH change, high salt concentration, and reducing
enzymes? 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 Inhibitor would cause a build up for product B, decrease
decrease given a specific inhibitor? A -> product C. Enzyme 3 and product D would not be created.
(enzyme 1) -> B -> (enzyme 2) -> C ->
(enzyme 3) -> D. Pretend Enzyme 2 is
inhibited.
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? Enzymes bind with certain substrate or type of substrate to
create a certain reaction
what is induced fit? Enzyme changes shape in enzyme-substrate complex to
facilitate formation of enzyme-product complex
what is kinase? Enzyme, adds phosphate group via phosphorlation
what is phosphatase? enzyme, removes phosphate group via dephosphorylation
with is an allosteric site? secondary site on an enzyme an inhibitor binds to via
non-competitive inhibition
what is competitive inhibition? enzyme substrate and inhibitor complex compete to bind with
enzyme's active site. no product formed when inhibitor binds
with enzyme.
what is non-competitive inhibition? inhibitor binds to allosteric site, not active site. Changes
shape of active site, preventing substrate from binding and
Questions & Answers Latest
2026/2027 with complete solution
What is the basic structure of an amino amino group (NH2 or NH3), carboxyl group (COO or COOH),
acid? What do they look like? alpha carbon (C), and variable group
How do you identify the 3 different types of Non-polar/hydrophobic - end with CH or "can't have" water.
side chains: non-polar/hydrophobic, polar, Polar - end with OH, SH, or NH. Charged - end with a charge
and charged?
what kinds of bonds do each of the 3 ionic, hydrophobic/non-polar, charged
different types of side chains make?
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 hydrophobic - temperature change, ionic - salt or decreased
type of bond? pH, hydrogen - temperature, change in pH, disulfide -
reducing agents
,what type of amino acid side chain leads to hydrophobic bonds
protein aggregration?
how do environmental changes affect Extreme temp can cause hydrogen bonds to break apart =
protein folding? 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 decrease activation energy and decrease reaction rate
activation energy?
what are the 4 steps of the enzymatic enzyme recognizes substrate, substrate attracts the enzyme;
cycle? enzyme-substrate complex is formed; enzyme-product
complex formed; product is released, enzyme recycled
how do environmental changes affect High heat, pH change, high salt concentration, and reducing
enzymes? 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 Inhibitor would cause a build up for product B, decrease
decrease given a specific inhibitor? A -> product C. Enzyme 3 and product D would not be created.
(enzyme 1) -> B -> (enzyme 2) -> C ->
(enzyme 3) -> D. Pretend Enzyme 2 is
inhibited.
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? Enzymes bind with certain substrate or type of substrate to
create a certain reaction
what is induced fit? Enzyme changes shape in enzyme-substrate complex to
facilitate formation of enzyme-product complex
what is kinase? Enzyme, adds phosphate group via phosphorlation
what is phosphatase? enzyme, removes phosphate group via dephosphorylation
with is an allosteric site? secondary site on an enzyme an inhibitor binds to via
non-competitive inhibition
what is competitive inhibition? enzyme substrate and inhibitor complex compete to bind with
enzyme's active site. no product formed when inhibitor binds
with enzyme.
what is non-competitive inhibition? inhibitor binds to allosteric site, not active site. Changes
shape of active site, preventing substrate from binding and
