WGU C785 FINAL EXAM WITH VERIFIED
CORRECT ANSWERS
What is the basic structure of an amino acid? What do they look like? - THE RIGHT
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? - THE RIGHT ANSWER Non-polar/hydrophobic - end with CH
or "can'thave" 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? - THE
RIGHT ANSWER ionic, hydrophobic/non-polar, charged
What are the 4 levels of protein structure? - THE RIGHT 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? - THE RIGHT
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? - THE RIGHT
ANSWERhydrophobic bonds
how do environmental changes affect protein folding? - THE RIGHT ANSWER
Extreme
temp can cause hydrogen bonds to break apart = malformation of protein folding
how do mutations affect protein structure? - THE RIGHT ANSWER Can cause
structure tochange. Protein loses form = loses function. May form a different protein.
What is an electron? - THE RIGHT ANSWER Negatively charged atom on outer ring
forbonding
What is energy: - THE RIGHT ANSWER Power derived fro chemical interaction
what are covalent bonds? - THE RIGHT ANSWER chemical bond, atoms share 1+
valenceelectrons
what is an ionic bond? - THE RIGHT ANSWER bond between positive and negative
what is a hydrogen bond? - THE RIGHT ANSWER weak bond between positive
andnegative
,with an amino? - THE RIGHT ANSWER piece of amino acid, NH2 or NH3
what is a carboyxl? - THE RIGHT ANSWER piece of amino acid, COO or COOH
What is hydrophobic? - THE RIGHT ANSWER Doesn't like water, end with CH
what is hydrophilic? - THE RIGHT ANSWER Water loving, end with OH, NH, or SH
what is disulfide bond? - THE RIGHT ANSWER strongest bond between
reduction agents,formed between SH's.
what are zwitterions? - THE RIGHT ANSWER amino with positive and negative
charges =overall charge of zero
what is a polypeptide - THE RIGHT ANSWER polymer of amino acids
What is dehydration synthesis? - THE RIGHT ANSWER Process of forming
peptide bonds
what is hydrolysis? - THE RIGHT ANSWER adding water to destroy bonds
what is an alpha helix? - THE RIGHT ANSWER twisted secondary
structure, formed byhydrogen bonds
what is a beta sheet? - THE RIGHT ANSWER folded second structure shape,
formed byhydrogen bonds
what is denaturation? - THE RIGHT ANSWER loss of shape duet o interruption of
chemicalbonds; occurs via extreme salt, temp, pH
what is aggregation? - THE RIGHT ANSWER clumping of inner or outer cellular
proteinscaused by misfolded proteins leading to diseases such as Alzheimers, ALS,
Parkinson's
how do enzymes catalyze reactions? - THE RIGHT ANSWER bind with substrates
todecrease activation energy required and decrease reaction rate
how do enzymes affect reaction rate and activation energy? - THE RIGHT
ANSWERdecrease activation energy and decrease reaction rate
what are the 4 steps of the enzymatic cycle? - THE RIGHT ANSWER enzyme
recognizessubstrate, substrate attracts the enzyme; enzyme-substrate complex is
formed; enzyme-product complex formed; product is released, enzyme recycled
how do environmental changes affect enzymes? - THE RIGHT ANSWER High
heat, pH change, high salt concentration, and reducing agents can cause an
enzyme to loseits form/lose function
what is a competitive inhibitor? - THE RIGHT ANSWER Mimics substrate
and takes itsplace on the active binding site
, what is a noncompetitive inhibitor? - THE RIGHT ANSWER Binds to allosteric site
causingactive 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. - THE RIGHT ANSWER Inhibitor would cause a build up for product
B, decreaseproduct C. Enzyme 3 and product D would not be created.
what is substrate? - THE RIGHT ANSWER the substance on which an enzyme acts
what is a product? - THE RIGHT ANSWER result of a reaction
what is an intermediate? - THE RIGHT ANSWER products produced in an
enzymepathway before final product
what is an active site? - THE RIGHT ANSWER location where substrate binds with
enzyme
what is enzyme specificity? - THE RIGHT ANSWER Enzymes bind with certain
substrate ortype of substrate to create a certain reaction
what is induced fit? - THE RIGHT ANSWER Enzyme changes shape in enzyme-
substratecomplex to facilitate formation of enzyme-product complex
what is kinase? - THE RIGHT ANSWER Enzyme, adds phosphate group via
phosphorlation
what is phosphatase? - THE RIGHT ANSWER enzyme, removes phosphate group
viadephosphorylation
with is an allosteric site? - THE RIGHT ANSWER secondary site on an enzyme
an inhibitorbinds to via non-competitive inhibition
what is competitive inhibition? - THE RIGHT ANSWER enzyme substrate and
inhibitor complex compete to bind with enzyme's active site. no product formed when
inhibitorbinds with enzyme.
what is non-competitive inhibition? - THE RIGHT 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? - THE RIGHT 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? -
THE RIGHT ANSWER C - cytosine, G - guanine, A - adenine, T - thyamine
what nucleotides/bases are used in RNA? - THE RIGHT ANSWER C - cytosine, G
-guanine, U - uracil, A - adenine
which nucleotides base-pair together in DNA? - THE RIGHT ANSWER T-A, G-C
CORRECT ANSWERS
What is the basic structure of an amino acid? What do they look like? - THE RIGHT
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? - THE RIGHT ANSWER Non-polar/hydrophobic - end with CH
or "can'thave" 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? - THE
RIGHT ANSWER ionic, hydrophobic/non-polar, charged
What are the 4 levels of protein structure? - THE RIGHT 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? - THE RIGHT
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? - THE RIGHT
ANSWERhydrophobic bonds
how do environmental changes affect protein folding? - THE RIGHT ANSWER
Extreme
temp can cause hydrogen bonds to break apart = malformation of protein folding
how do mutations affect protein structure? - THE RIGHT ANSWER Can cause
structure tochange. Protein loses form = loses function. May form a different protein.
What is an electron? - THE RIGHT ANSWER Negatively charged atom on outer ring
forbonding
What is energy: - THE RIGHT ANSWER Power derived fro chemical interaction
what are covalent bonds? - THE RIGHT ANSWER chemical bond, atoms share 1+
valenceelectrons
what is an ionic bond? - THE RIGHT ANSWER bond between positive and negative
what is a hydrogen bond? - THE RIGHT ANSWER weak bond between positive
andnegative
,with an amino? - THE RIGHT ANSWER piece of amino acid, NH2 or NH3
what is a carboyxl? - THE RIGHT ANSWER piece of amino acid, COO or COOH
What is hydrophobic? - THE RIGHT ANSWER Doesn't like water, end with CH
what is hydrophilic? - THE RIGHT ANSWER Water loving, end with OH, NH, or SH
what is disulfide bond? - THE RIGHT ANSWER strongest bond between
reduction agents,formed between SH's.
what are zwitterions? - THE RIGHT ANSWER amino with positive and negative
charges =overall charge of zero
what is a polypeptide - THE RIGHT ANSWER polymer of amino acids
What is dehydration synthesis? - THE RIGHT ANSWER Process of forming
peptide bonds
what is hydrolysis? - THE RIGHT ANSWER adding water to destroy bonds
what is an alpha helix? - THE RIGHT ANSWER twisted secondary
structure, formed byhydrogen bonds
what is a beta sheet? - THE RIGHT ANSWER folded second structure shape,
formed byhydrogen bonds
what is denaturation? - THE RIGHT ANSWER loss of shape duet o interruption of
chemicalbonds; occurs via extreme salt, temp, pH
what is aggregation? - THE RIGHT ANSWER clumping of inner or outer cellular
proteinscaused by misfolded proteins leading to diseases such as Alzheimers, ALS,
Parkinson's
how do enzymes catalyze reactions? - THE RIGHT ANSWER bind with substrates
todecrease activation energy required and decrease reaction rate
how do enzymes affect reaction rate and activation energy? - THE RIGHT
ANSWERdecrease activation energy and decrease reaction rate
what are the 4 steps of the enzymatic cycle? - THE RIGHT ANSWER enzyme
recognizessubstrate, substrate attracts the enzyme; enzyme-substrate complex is
formed; enzyme-product complex formed; product is released, enzyme recycled
how do environmental changes affect enzymes? - THE RIGHT ANSWER High
heat, pH change, high salt concentration, and reducing agents can cause an
enzyme to loseits form/lose function
what is a competitive inhibitor? - THE RIGHT ANSWER Mimics substrate
and takes itsplace on the active binding site
, what is a noncompetitive inhibitor? - THE RIGHT ANSWER Binds to allosteric site
causingactive 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. - THE RIGHT ANSWER Inhibitor would cause a build up for product
B, decreaseproduct C. Enzyme 3 and product D would not be created.
what is substrate? - THE RIGHT ANSWER the substance on which an enzyme acts
what is a product? - THE RIGHT ANSWER result of a reaction
what is an intermediate? - THE RIGHT ANSWER products produced in an
enzymepathway before final product
what is an active site? - THE RIGHT ANSWER location where substrate binds with
enzyme
what is enzyme specificity? - THE RIGHT ANSWER Enzymes bind with certain
substrate ortype of substrate to create a certain reaction
what is induced fit? - THE RIGHT ANSWER Enzyme changes shape in enzyme-
substratecomplex to facilitate formation of enzyme-product complex
what is kinase? - THE RIGHT ANSWER Enzyme, adds phosphate group via
phosphorlation
what is phosphatase? - THE RIGHT ANSWER enzyme, removes phosphate group
viadephosphorylation
with is an allosteric site? - THE RIGHT ANSWER secondary site on an enzyme
an inhibitorbinds to via non-competitive inhibition
what is competitive inhibition? - THE RIGHT ANSWER enzyme substrate and
inhibitor complex compete to bind with enzyme's active site. no product formed when
inhibitorbinds with enzyme.
what is non-competitive inhibition? - THE RIGHT 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? - THE RIGHT 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? -
THE RIGHT ANSWER C - cytosine, G - guanine, A - adenine, T - thyamine
what nucleotides/bases are used in RNA? - THE RIGHT ANSWER C - cytosine, G
-guanine, U - uracil, A - adenine
which nucleotides base-pair together in DNA? - THE RIGHT ANSWER T-A, G-C
