WGU C785 Biochemistry (Latest 2026 / 2027) Complete Exam Questions and 100% Correct Answers (Verified Pass)

WGU C785 Biochemistry (Latest 2026 /
2027) Complete Exam Questions and 100%
Correct Answers (Verified Pass)
• How do you identify the 3 different types of side chains: non-polar/hydrophobic, polar,
and charged? -✓✓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? -✓✓ionic,
hydrophobic/non-polar, charged

• 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 aggregration? -✓✓hydrophobic
bonds

• 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 energy? -✓✓decrease activation
energy and decrease reaction rate

• 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

• 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. -
✓✓Inhibitor would cause a build up for product B, decrease product C. Enzyme 3 and
product D would not be created.

• 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 making product

• what is feedback inhibition? -✓✓End product sends feedback to beginning of enzyme
pathway inhibiting 1st enzyme via noncompetitive inhibition

• what nucleotides/bases are used in DNA? what are their abbreviations/full names? -
✓✓C - cytosine, G - guanine, A - adenine, T - thyamine

• what nucleotides/bases are used in RNA? -✓✓C - cytosine, G - guanine, U - uracil, A -
adenine