WGU C785 Questions and Answers
Already Passed
What is the basic structure of an amino acid? What do they look like? ✔✔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? ✔✔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? ✔✔ionic,
hydrophobic/non-polar, charged
What are the 4 levels of protein structure? ✔✔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? ✔✔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? ✔✔hydrophobic bonds
,how do environmental changes affect protein folding? ✔✔Extreme temp can cause hydrogen
bonds to break apart = malformation of protein folding
how do mutations affect protein structure? ✔✔Can cause structure to change. Protein loses form
= loses function. May form a different protein.
What is an electron? ✔✔Negatively charged atom on outer ring for bonding
What is energy: ✔✔Power derived fro chemical interaction
what are covalent bonds? ✔✔chemical bond, atoms share 1+ valence electrons
what is an ionic bond? ✔✔bond between positive and negative
what is a hydrogen bond? ✔✔weak bond between positive and negative
with an amino? ✔✔piece of amino acid, NH2 or NH3
what is a carboyxl? ✔✔piece of amino acid, COO or COOH
What is hydrophobic? ✔✔Doesn't like water, end with CH
,what is hydrophilic? ✔✔Water Lovering, end with OH, NH, or SH
what is disulfide bond? ✔✔strongest bond between reduction agents, formed between SH's.
what are zwitterions? ✔✔amino with positive and negative charges = overall charge of zero
what is a polypeptide ✔✔polymer of amino acids
What is dehydration synthesis? ✔✔Process of forming peptide bonds
what is hydrolysis? ✔✔adding water to destroy bonds
what is an alpha helix? ✔✔twisted secondary structure, formed by hydrogen bonds
what is a beta sheet? ✔✔folded second structure shape, formed by hydrogen bonds
what is denaturation? ✔✔loss of shape duet o interruption of chemical bonds; occurs via extreme
salt, temp, pH
what is aggregation? ✔✔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? ✔✔bind with substrates to decrease activation energy
required and decrease reaction rate
how do enzymes affect reaction rate and activation energy? ✔✔decrease activation energy and
decrease reaction rate
what are the 4 steps of the enzymatic cycle? ✔✔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? ✔✔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? ✔✔Mimics substrate and takes its place on the active binding site
what is a noncompetitive inhibitor? ✔✔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. ✔✔Inhibitor would cause a
build up for product B, decrease product C. Enzyme 3 and product D would not be created.
Already Passed
What is the basic structure of an amino acid? What do they look like? ✔✔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? ✔✔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? ✔✔ionic,
hydrophobic/non-polar, charged
What are the 4 levels of protein structure? ✔✔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? ✔✔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? ✔✔hydrophobic bonds
,how do environmental changes affect protein folding? ✔✔Extreme temp can cause hydrogen
bonds to break apart = malformation of protein folding
how do mutations affect protein structure? ✔✔Can cause structure to change. Protein loses form
= loses function. May form a different protein.
What is an electron? ✔✔Negatively charged atom on outer ring for bonding
What is energy: ✔✔Power derived fro chemical interaction
what are covalent bonds? ✔✔chemical bond, atoms share 1+ valence electrons
what is an ionic bond? ✔✔bond between positive and negative
what is a hydrogen bond? ✔✔weak bond between positive and negative
with an amino? ✔✔piece of amino acid, NH2 or NH3
what is a carboyxl? ✔✔piece of amino acid, COO or COOH
What is hydrophobic? ✔✔Doesn't like water, end with CH
,what is hydrophilic? ✔✔Water Lovering, end with OH, NH, or SH
what is disulfide bond? ✔✔strongest bond between reduction agents, formed between SH's.
what are zwitterions? ✔✔amino with positive and negative charges = overall charge of zero
what is a polypeptide ✔✔polymer of amino acids
What is dehydration synthesis? ✔✔Process of forming peptide bonds
what is hydrolysis? ✔✔adding water to destroy bonds
what is an alpha helix? ✔✔twisted secondary structure, formed by hydrogen bonds
what is a beta sheet? ✔✔folded second structure shape, formed by hydrogen bonds
what is denaturation? ✔✔loss of shape duet o interruption of chemical bonds; occurs via extreme
salt, temp, pH
what is aggregation? ✔✔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? ✔✔bind with substrates to decrease activation energy
required and decrease reaction rate
how do enzymes affect reaction rate and activation energy? ✔✔decrease activation energy and
decrease reaction rate
what are the 4 steps of the enzymatic cycle? ✔✔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? ✔✔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? ✔✔Mimics substrate and takes its place on the active binding site
what is a noncompetitive inhibitor? ✔✔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. ✔✔Inhibitor would cause a
build up for product B, decrease product C. Enzyme 3 and product D would not be created.
