Test Bank for
WGU C785 BIOCHEMISTRY
** Expert-Verified Explanation
** Questions with Verified Answer
** New Edition | 2026-2027 Updated
** 100% Guaranteed Pass
** 100% Correct Answers | Graded A+
,What is the basic structure of an amino acid? What do amino group (NH2 or NH3), carboxyl group (COO or COOH), alpha carbon (C),
they look like? and variable group
How do you identify the 3 different types of side chains: Non-polar/hydrophobic - end with CH or "can't have" water. Polar - end with OH,
non-polar/hydrophobic, polar, and charged? SH, or NH. Charged - end with a charge
what kinds of bonds do each of the 3 different types of ionic, hydrophobic/non-polar, charged
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 type of bond? 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 hydrophobic bonds
aggregration?
how do environmental changes affect protein folding? Extreme temp can cause hydrogen bonds to break apart = 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 activation decrease activation energy and decrease reaction rate
energy?
what are the 4 steps of the enzymatic cycle? 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? 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? 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
WGU C785 BIOCHEMISTRY
** Expert-Verified Explanation
** Questions with Verified Answer
** New Edition | 2026-2027 Updated
** 100% Guaranteed Pass
** 100% Correct Answers | Graded A+
,What is the basic structure of an amino acid? What do amino group (NH2 or NH3), carboxyl group (COO or COOH), alpha carbon (C),
they look like? and variable group
How do you identify the 3 different types of side chains: Non-polar/hydrophobic - end with CH or "can't have" water. Polar - end with OH,
non-polar/hydrophobic, polar, and charged? SH, or NH. Charged - end with a charge
what kinds of bonds do each of the 3 different types of ionic, hydrophobic/non-polar, charged
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 type of bond? 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 hydrophobic bonds
aggregration?
how do environmental changes affect protein folding? Extreme temp can cause hydrogen bonds to break apart = 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 activation decrease activation energy and decrease reaction rate
energy?
what are the 4 steps of the enzymatic cycle? 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? 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? 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
