What is the basic structure of an amino acid? What do they look like? - correct
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? - correct 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? - correct
answer ionic, hydrophobic/non-polar, charged
What are the 4 levels of protein structure? - correct 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? - correct 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? - correct answer
hydrophobic bonds
how do environmental changes affect protein folding? - correct answer Extreme
temp can cause hydrogen bonds to break apart = malformation of protein folding
how do mutations affect protein structure? - correct answer Can cause structure to
change. Protein loses form = loses function. May form a different protein.
What is an electron? - correct answer Negatively charged atom on outer ring for
bonding
What is energy: - correct answer Power derived fro chemical interaction
what are covalent bonds? - correct answer chemical bond, atoms share 1+ valence
electrons
what is an ionic bond? - correct answer bond between positive and negative
what is a hydrogen bond? - correct answer weak bond between positive and
negative
,with an amino? - correct answer piece of amino acid, NH2 or NH3
what is a carboyxl? - correct answer piece of amino acid, COO or COOH
What is hydrophobic? - correct answer Doesn't like water, end with CH
what is hydrophilic? - correct answer Water loving, end with OH, NH, or SH
what is disulfide bond? - correct answer strongest bond between reduction agents,
formed between SH's.
what are zwitterions? - correct answer amino with positive and negative charges =
overall charge of zero
what is a polypeptide - correct answer polymer of amino acids
What is dehydration synthesis? - correct answer Process of forming peptide bonds
what is hydrolysis? - correct answer adding water to destroy bonds
what is an alpha helix? - correct answer twisted secondary structure, formed by
hydrogen bonds
what is a beta sheet? - correct answer folded second structure shape, formed by
hydrogen bonds
what is denaturation? - correct answer loss of shape duet o interruption of chemical
bonds; occurs via extreme salt, temp, pH
what is aggregation? - correct 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? - correct answer bind with substrates to
decrease activation energy required and decrease reaction rate
how do enzymes affect reaction rate and activation energy? - correct answer
decrease activation energy and decrease reaction rate
what are the 4 steps of the enzymatic cycle? - correct 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? - correct 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? - correct answer Mimics substrate and takes its
place on the active binding site
, what is a noncompetitive inhibitor? - correct 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. - correct 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? - correct answer the substance on which an enzyme acts
what is a product? - correct answer result of a reaction
what is an intermediate? - correct answer products produced in an enzyme
pathway before final product
what is an active site? - correct answer location where substrate binds with enzyme
what is enzyme specificity? - correct answer Enzymes bind with certain substrate or
type of substrate to create a certain reaction
what is induced fit? - correct answer Enzyme changes shape in enzyme-substrate
complex to facilitate formation of enzyme-product complex
what is kinase? - correct answer Enzyme, adds phosphate group via
phosphorlation
what is phosphatase? - correct answer enzyme, removes phosphate group via
dephosphorylation
with is an allosteric site? - correct answer secondary site on an enzyme an inhibitor
binds to via non-competitive inhibition
what is competitive inhibition? - correct 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? - correct 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? - correct 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? -
correct answer C - cytosine, G - guanine, A - adenine, T - thyamine
what nucleotides/bases are used in RNA? - correct answer C - cytosine, G -
guanine, U - uracil, A - adenine
which nucleotides base-pair together in DNA? - correct answer T-A, G-C
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? - correct 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? - correct
answer ionic, hydrophobic/non-polar, charged
What are the 4 levels of protein structure? - correct 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? - correct 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? - correct answer
hydrophobic bonds
how do environmental changes affect protein folding? - correct answer Extreme
temp can cause hydrogen bonds to break apart = malformation of protein folding
how do mutations affect protein structure? - correct answer Can cause structure to
change. Protein loses form = loses function. May form a different protein.
What is an electron? - correct answer Negatively charged atom on outer ring for
bonding
What is energy: - correct answer Power derived fro chemical interaction
what are covalent bonds? - correct answer chemical bond, atoms share 1+ valence
electrons
what is an ionic bond? - correct answer bond between positive and negative
what is a hydrogen bond? - correct answer weak bond between positive and
negative
,with an amino? - correct answer piece of amino acid, NH2 or NH3
what is a carboyxl? - correct answer piece of amino acid, COO or COOH
What is hydrophobic? - correct answer Doesn't like water, end with CH
what is hydrophilic? - correct answer Water loving, end with OH, NH, or SH
what is disulfide bond? - correct answer strongest bond between reduction agents,
formed between SH's.
what are zwitterions? - correct answer amino with positive and negative charges =
overall charge of zero
what is a polypeptide - correct answer polymer of amino acids
What is dehydration synthesis? - correct answer Process of forming peptide bonds
what is hydrolysis? - correct answer adding water to destroy bonds
what is an alpha helix? - correct answer twisted secondary structure, formed by
hydrogen bonds
what is a beta sheet? - correct answer folded second structure shape, formed by
hydrogen bonds
what is denaturation? - correct answer loss of shape duet o interruption of chemical
bonds; occurs via extreme salt, temp, pH
what is aggregation? - correct 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? - correct answer bind with substrates to
decrease activation energy required and decrease reaction rate
how do enzymes affect reaction rate and activation energy? - correct answer
decrease activation energy and decrease reaction rate
what are the 4 steps of the enzymatic cycle? - correct 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? - correct 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? - correct answer Mimics substrate and takes its
place on the active binding site
, what is a noncompetitive inhibitor? - correct 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. - correct 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? - correct answer the substance on which an enzyme acts
what is a product? - correct answer result of a reaction
what is an intermediate? - correct answer products produced in an enzyme
pathway before final product
what is an active site? - correct answer location where substrate binds with enzyme
what is enzyme specificity? - correct answer Enzymes bind with certain substrate or
type of substrate to create a certain reaction
what is induced fit? - correct answer Enzyme changes shape in enzyme-substrate
complex to facilitate formation of enzyme-product complex
what is kinase? - correct answer Enzyme, adds phosphate group via
phosphorlation
what is phosphatase? - correct answer enzyme, removes phosphate group via
dephosphorylation
with is an allosteric site? - correct answer secondary site on an enzyme an inhibitor
binds to via non-competitive inhibition
what is competitive inhibition? - correct 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? - correct 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? - correct 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? -
correct answer C - cytosine, G - guanine, A - adenine, T - thyamine
what nucleotides/bases are used in RNA? - correct answer C - cytosine, G -
guanine, U - uracil, A - adenine
which nucleotides base-pair together in DNA? - correct answer T-A, G-C
