WGU C785 BIOCHEMISTRY FINAL OA EXAM REAL EXAM
QUESTIONS AND CORRECT ANSWERS|AGRADE(COMPLETE
EXAM)
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
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
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
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
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.
- 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? - ANSWER: the substance on which an enzyme acts
what is a product? - ANSWER: result of a reaction
what is an intermediate? - ANSWER: products produced in an enzyme pathway
before final product
what is an active site? - ANSWER: location where substrate binds with enzyme
what is enzyme specificity? - ANSWER: Enzymes bind with certain substrate or type
of substrate to create a certain reaction
what is induced fit? - ANSWER: Enzyme changes shape in enzyme-substrate complex
to facilitate formation of enzyme-product complex
what is kinase? - ANSWER: Enzyme, adds phosphate group via phosphorlation
what is phosphatase? - ANSWER: enzyme, removes phosphate group via
dephosphorylation
with is an allosteric site? - ANSWER: secondary site on an enzyme an inhibitor binds
to via non-competitive inhibition
what is competitive inhibition? - ANSWER: 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? - ANSWER: inhibitor binds to allosteric site, not
active site. Changes shape of active site, preventing substrate from binding and
making product
what is feedback inhibition? - ANSWER: 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? -
ANSWER: C - cytosine, G - guanine, A - adenine, T - thyamine
QUESTIONS AND CORRECT ANSWERS|AGRADE(COMPLETE
EXAM)
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
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
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
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
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.
- 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? - ANSWER: the substance on which an enzyme acts
what is a product? - ANSWER: result of a reaction
what is an intermediate? - ANSWER: products produced in an enzyme pathway
before final product
what is an active site? - ANSWER: location where substrate binds with enzyme
what is enzyme specificity? - ANSWER: Enzymes bind with certain substrate or type
of substrate to create a certain reaction
what is induced fit? - ANSWER: Enzyme changes shape in enzyme-substrate complex
to facilitate formation of enzyme-product complex
what is kinase? - ANSWER: Enzyme, adds phosphate group via phosphorlation
what is phosphatase? - ANSWER: enzyme, removes phosphate group via
dephosphorylation
with is an allosteric site? - ANSWER: secondary site on an enzyme an inhibitor binds
to via non-competitive inhibition
what is competitive inhibition? - ANSWER: 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? - ANSWER: inhibitor binds to allosteric site, not
active site. Changes shape of active site, preventing substrate from binding and
making product
what is feedback inhibition? - ANSWER: 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? -
ANSWER: C - cytosine, G - guanine, A - adenine, T - thyamine
