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WGU C785 Final Exam 2024 With All The Correct Answers
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WGU C785 Final Exam 2024 With All The Correct Answers
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WGU C785 FINAL EXAM WITHCORRECT ANSWERS(Biochemistry Units
2-7)
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
,WGU C785 FINAL EXAM WITH
CORRECT ANSWERS(Biochemistry Units
2-7)
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
,WGU C785 FINAL EXAM WITH
CORRECT ANSWERS(Biochemistry Units
2-7)
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.
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
, WGU C785 FINAL EXAM WITH
CORRECT ANSWERS(Biochemistry Units
2-7)
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
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