WGU C785 Final Exam With All The
Correct Answers|| 100% pass
What is the fundamental structure of an amino acid? How do they look? amino group
(NH2 or NH3), carboxyl group (COO or COOH), alpha carbon (C), and variable group.
How do you distinguish the three sorts of side chains: non-polar/hydrophobic, polar, and
charged? Non-polar/hydrophobic - ends in CH or "can't have" water. Polar compounds
terminate with OH, SH, or NH. Charged - finish with a charge
What kind of bonds do each of the three types of side chains form? Ionic,
hydrophobic/non-polar, charged.
What are the four levels of protein structure? : Primary - linear structure, secondary -
folded into helix or pleated sheet induced by hydrogen bonding, tertiary - 3D structure
generated by side chain interactions, and quaternary - 1+ amino acid chains combine =
many subunits MUST have 1+ subunit
What environmental change disrupts each sort of bond? Hydrophobic - temperature
change, ionic - salt or lowered pH, hydrogen - temperature, pH change, and disulfide -
reducing agents
What sort of amino acid side chain promotes protein aggregation? : Hydrophobic bonds
How do environmental changes influence protein folding? Extreme temperatures can
cause hydrogen bonds to break away, resulting in malformation of protein folding.
How do mutations influence protein structure? : Can cause structural changes. Protein
loses shape, which means it loses function. It is possible that a new protein will develop.
What is an electron? : A negatively charged atom on the outer ring for bonding.
What is energy? Power derived from chemical interactions.
,What are covalent bonds? In chemical bond, atoms share one or more valence electrons
What is an ionic bond? The connection between positive and negative.
What is a hydrogen bond? a weak link between positive and negative.
With an amino? : a fragment of amino acid (NH2 or NH3)
What is a Carboyxl? a fragment of amino acid, COO or COOH
What is hydrophobic? : Does not like water, ends with CH.
What exactly does "hydrophilic" mean? : Water-loving, ending with OH, NH, or SH
What is a disulfide bond? : The strongest link between reduction agents, created by SHs.
What is a zwitterion? : amino with positive and negative charges = total charge of zero.
What is a polypeptide? A polymer of amino acids.
What is dehydration synthesis? : The process of creating peptide connections
What is hydrolysis? : introducing water to break ties
What is an alpha helix? A twisted secondary structure formed by hydrogen bonding.
What is a beta sheet? The hydrogen bonds generate a folded second structure shape.
What is denaturation? : loss of shape due to breakage of chemical bonds; happens through
excessive salt, temperature, and pH.
What is aggregation? Misfolded proteins produce clumping of inner or outer cellular
proteins, which leads to disorders including Alzheimer's, ALS, and Parkinson's.
How can enzymes catalyse reactions? : bind with substrates to lower activation energy and
reaction rate.
How do enzymes influence reaction rates and activation energies? decrease activation
energy and reaction rate.
,What are the four steps of the enzymatic cycle? Enzyme detects substrate; substrate
attracts enzyme; enzyme-substrate complex is formed; enzyme-product complex created;
product is released; enzyme recycled.
How do environmental changes influence enzymes? High heat, pH changes, high salt
concentrations, and reducing chemicals can cause an enzyme to lose its shape or function.
What is a competitive inhibitor? It mimics the substrate and takes its place at the active
binding site.
What is a non-competitive inhibitor? Binds to the allosteric site, causing the active site to
change shape, preventing the substrate from engaging with the enzyme.
What molecules rise or decrease in response to a specific inhibitor? A -> (enzyme 1), B ->
(enzyme 2), C -> (enzyme 3), and D. Assume Enzyme 2 is inhibited. The inhibitor would
induce a buildup of product B and decrease product C. Enzyme 3 and Product D would
not be produced.
What is a substrate? : the material on which an enzyme acts
What is a product? : the outcome of a reaction.
, What is an intermediate? : products created in an enzyme route before the final product.
What constitutes an active site? The site where the substrate attaches to the enzyme
What is enzyme specificity? Enzymes bind with certain substrates or types of substrates to
produce a specific reaction.
What is an induced fit? The enzyme changes shape in the enzyme-substrate complex to aid
the development of the enzyme-product complex.
What is kinase? : Enzyme that adds phosphate group through phosphorlation
What is phosphatase? An enzyme that eliminates phosphate group through
dephosphorylation
What constitutes an allosteric site? A secondary site on an enzyme where an inhibitor
binds through non-competitive inhibition.
Correct Answers|| 100% pass
What is the fundamental structure of an amino acid? How do they look? amino group
(NH2 or NH3), carboxyl group (COO or COOH), alpha carbon (C), and variable group.
How do you distinguish the three sorts of side chains: non-polar/hydrophobic, polar, and
charged? Non-polar/hydrophobic - ends in CH or "can't have" water. Polar compounds
terminate with OH, SH, or NH. Charged - finish with a charge
What kind of bonds do each of the three types of side chains form? Ionic,
hydrophobic/non-polar, charged.
What are the four levels of protein structure? : Primary - linear structure, secondary -
folded into helix or pleated sheet induced by hydrogen bonding, tertiary - 3D structure
generated by side chain interactions, and quaternary - 1+ amino acid chains combine =
many subunits MUST have 1+ subunit
What environmental change disrupts each sort of bond? Hydrophobic - temperature
change, ionic - salt or lowered pH, hydrogen - temperature, pH change, and disulfide -
reducing agents
What sort of amino acid side chain promotes protein aggregation? : Hydrophobic bonds
How do environmental changes influence protein folding? Extreme temperatures can
cause hydrogen bonds to break away, resulting in malformation of protein folding.
How do mutations influence protein structure? : Can cause structural changes. Protein
loses shape, which means it loses function. It is possible that a new protein will develop.
What is an electron? : A negatively charged atom on the outer ring for bonding.
What is energy? Power derived from chemical interactions.
,What are covalent bonds? In chemical bond, atoms share one or more valence electrons
What is an ionic bond? The connection between positive and negative.
What is a hydrogen bond? a weak link between positive and negative.
With an amino? : a fragment of amino acid (NH2 or NH3)
What is a Carboyxl? a fragment of amino acid, COO or COOH
What is hydrophobic? : Does not like water, ends with CH.
What exactly does "hydrophilic" mean? : Water-loving, ending with OH, NH, or SH
What is a disulfide bond? : The strongest link between reduction agents, created by SHs.
What is a zwitterion? : amino with positive and negative charges = total charge of zero.
What is a polypeptide? A polymer of amino acids.
What is dehydration synthesis? : The process of creating peptide connections
What is hydrolysis? : introducing water to break ties
What is an alpha helix? A twisted secondary structure formed by hydrogen bonding.
What is a beta sheet? The hydrogen bonds generate a folded second structure shape.
What is denaturation? : loss of shape due to breakage of chemical bonds; happens through
excessive salt, temperature, and pH.
What is aggregation? Misfolded proteins produce clumping of inner or outer cellular
proteins, which leads to disorders including Alzheimer's, ALS, and Parkinson's.
How can enzymes catalyse reactions? : bind with substrates to lower activation energy and
reaction rate.
How do enzymes influence reaction rates and activation energies? decrease activation
energy and reaction rate.
,What are the four steps of the enzymatic cycle? Enzyme detects substrate; substrate
attracts enzyme; enzyme-substrate complex is formed; enzyme-product complex created;
product is released; enzyme recycled.
How do environmental changes influence enzymes? High heat, pH changes, high salt
concentrations, and reducing chemicals can cause an enzyme to lose its shape or function.
What is a competitive inhibitor? It mimics the substrate and takes its place at the active
binding site.
What is a non-competitive inhibitor? Binds to the allosteric site, causing the active site to
change shape, preventing the substrate from engaging with the enzyme.
What molecules rise or decrease in response to a specific inhibitor? A -> (enzyme 1), B ->
(enzyme 2), C -> (enzyme 3), and D. Assume Enzyme 2 is inhibited. The inhibitor would
induce a buildup of product B and decrease product C. Enzyme 3 and Product D would
not be produced.
What is a substrate? : the material on which an enzyme acts
What is a product? : the outcome of a reaction.
, What is an intermediate? : products created in an enzyme route before the final product.
What constitutes an active site? The site where the substrate attaches to the enzyme
What is enzyme specificity? Enzymes bind with certain substrates or types of substrates to
produce a specific reaction.
What is an induced fit? The enzyme changes shape in the enzyme-substrate complex to aid
the development of the enzyme-product complex.
What is kinase? : Enzyme that adds phosphate group through phosphorlation
What is phosphatase? An enzyme that eliminates phosphate group through
dephosphorylation
What constitutes an allosteric site? A secondary site on an enzyme where an inhibitor
binds through non-competitive inhibition.
