WGU C785 Final Exam with All the Correct Answers
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 loving, 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
what nucleotides/bases are used in RNA? -Answer- C - cytosine, G - guanine, U -
uracil, A - adenine
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 loving, 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
what nucleotides/bases are used in RNA? -Answer- C - cytosine, G - guanine, U -
uracil, A - adenine
