Transcript answer - RogueBCHES.com

ROGUE
Biochemistry Jeopardy
Find the
Penis
Sh*t That
Came Out of
My Mouth
I’ve Got 99
Upshots, But a
BCH Ain’t One
10
10
10
10
20
20
20
20
20
30
30
30
30
30
40
40
40
40
40
50
50
50
50
50
The BIG
Picture
I Like Big
Bottoms and I
cannot Line
10
The BIG Picture – 10 Points
1
ANSWER:
L-aspartate
1a
ANSWER:
L-serine
The BIG Picture – 20 Points
2
ANSWER:
L-lysine
2a
ANSWER:
L-histidine
The BIG Picture – 30 Points
3
ANSWER:
L-leucine
3a
ANSWER:
L-methionine
The BIG Picture – 40 Points
4
ANSWER:
L-proline
4a
ANSWER:
L-asparagine
The BIG Picture – 50 Points
5
ANSWER:
Beta-sheet
5aa
ANSWER:
acetylcholine
I Like Big Bottoms and I Cannot Line – 10 Points
a) A _______________is a graph of the conformational torsion angles phi and
psi for the residues in a protein or peptide, a map of the structure of the
polypeptide backbone.
b) The ____________ approximation postulates that a constant input feed of
substrate is supplied whose rate equals that of product formation.
c) What chemical group does coenzyme A typically carry in the course of its
biochemical function?
d) A coenzyme is either a loosely bound cosubstrate or strongly bound
____________.
ANSWER:
a) Ramachandran plot
b) steady state
c) acetyl??
d) prosthetic group
I Like Big Bottoms and I Cannot Line – 20 Points
a) The coenzyme bound carbohydrates UDP-galactose and glucose are
required to synthesize __________.
b) A _______________ attacks an electropositive site in its role in a chemical
(enzymatic) reaction
c) A decrease in the activity of an enzyme as a result of binding of a product
from the reaction in question or subsequent reactions is referred to as
___________________.
d) . The _________________ (or double reciprocal) equation defines
parameters that are used to characterize the kinetics of an enzyme.
ANSWER:
a) lactose
b) nucleophile
c) feedback inhibition
d) Lineweaver-Burk
I Like Big Bottoms and I Cannot Line– 30 Points
a) The ______________ of an enzymatic catalysis reaction is the rate achieved
when it is saturated with substrate.
b) What amino acid and functional group in the esterase site of acetylcholine
esterase reacts with the substrate?
c) The most common amino acid used by enzymes to carry out ____________
is histidine.
d) The (vitamin) ________________ is required to synthesize coenzyme NAD+
for use in metabolic redox reactions.
ANSWER:
a) maximum velocity
b) serine hydroxylate
c) acid-base catalysis
d) niacin
I Like Big Bottoms and I Cannot Line – 40 Points
a) ____________ functions in transducing the signal of a photon of light into a
chemically recognizable form
b) Which two amino acids are modified in the reactions catalyzed by cyclin
kinase?
c) ___________ is the substrate concentration when Vo = Vmax/2.
d) The _______________ interaction describes the relation between
interatomic distances, electronic charge, solution dielectric and free energies.
ANSWER:
a) cis-retinal
b) tyrosine, threonine
c) Michaelis constant
d) van der Waals
I Like Big Bottoms and I Cannot Line – 50 Points
a) (a) Protein _______ structure defines the packing of helices, sheets, turns, etc. (b)
Protein primary structure defines the _________. (c) Protein ________ structure defines
the relation among subunits in a multisubunit lattice. (d) Protein _________ structure
defines the motifs formed by short-range interactions between amino acids.
b) Two internal factors that limit the velocity of an enzymatic reaction are _________ and
_________.
c) A chaotropic agent induces denaturation of proteins by disturbing the
___________________.
d) Two examples of irreversible factors that control the catalytic capability of an enzyme
are: ______________, ________________
ANSWER:
a) (a) tertiary, (b) amino acid sequence, (c)
quaternary, (d) secondary
b) hydrophobic effect, H-bonding, disulfide
bonds, van der Waals forces, ionic bonds (salt
bridges) or dipole-dipole interactions
c) hydrophobic effect
d) covalent modification, proteolysis, irreversible
inhibitors
Find the Penis – 10 Points
DIRECTIONS:
Name each structure in order from left to right.
ANSWER:
glycerol
glyceraldehyde
glycerate
2,3-bisphosphoglycerate
The penis: me
Find the Penis – 20 Points
DIRECTIONS: Identify each of the following structures: a, b, c, and d.
ANSWER:
a) activator
b) inhibitor
c) active site
d) allosteric inhibitor site
The penis: inhibitor (or most creative)
Find the Penis – 30 Points
DIRECTIONS: Identify each of the following structures: a, b, c, and d.
ANSWER:
a) glycogen phosphorylase b
b) glycogen phosphorylase kinase
c) glycogen phosphorylase a
d) glycogen phosphorylase phosphatase
The penis: Novice: glycogen phospohorylase,
Intermediate: phosphate and arginines, Advanced: same
as intermediate but emphasis on “salt bridge”
Find the Penis– 40 Points
DIRECTIONS: Identify each of the following structures: a, b, c, and d.
ANSWER:
a) aspartate
b) histidine
c) serine
d) specificity pocket
The penis: Awarded based on creativity
Find the Penis – 50 Points
DIRECTIONS: Identify each of the following structures: a, b, c, and d.
ANSWER:
a) glutamate
b) alpha-ketoglutarate
c) oxaloacetate
d) aspartate
The penis: Awarded based on creativity
Sh*t That Came Out of My Mouth– 10 Points
a) A _______________ interaction involves polar O, N or both and the atom for
which it is named, and constitutes one of the important protein stabilization
elements.
b) Pyridine aldoximine methiodide (PAM) reactivates __________________,
functioning as a nerve gas antidote.
c) The coenzyme ____________________________ is required to incorporate
the methyl group into thymidine, a necessary prerequisite for the production of
DNA.
d) Cyclin kinase regulates entry and exit from mitosis by catalyzing a ________
___________ reaction.
ANSWER:
a) hydrogen bond
b) acetylcholine esterase
c) N5,N10-methylenetetrahydrofolate
d) covalent modification
Double: What pneumonic was used to remember the structure for PAM
(draw and explain)!
Triple: How are the different hydrogen bond types like relationships
Sh*t That Came Out of My Mouth– 20 Points
a) An act of catalysis does not change an enzyme and lowers the
___________________ of the associated reaction.
b) The catalytic rate constant of an enzyme is abbreviated as _________.
c) List the two “chemical modes of catalysis”.
d) ___________________ of enzyme catalysis occurs when the inhibitor only
binds to the enzyme substrate complex.
ANSWER:
a) transition state free energy
b) kcat
c) acid-base, covalent
d) Uncompetitive inhibition
Double: Transition state free energy was used to describe a real world
transition. What was it and how does it demonstrate that women are hateful,
hateful liars?
Triple: What sexual activity can one get another to do when you reach the
substrate concentration required to achieve the maximum initial rate?
Sh*t That Came Out of My Mouth– 30 Points
a) The most typically cited currency of energy in metabolism is
________________.
b) . The _____________ is the characteristic speed of an enzyme’s kinetics
extrapolated to the time when a defined amount of substrate is added to the
enzyme solution
c) A catalytic triad of amino acids is typically present in ______________ .
d) The bisubstrate-enzyme ping-pong reaction is used by _____________ in
the exchange of an amino group for a carbonyl group between two
progressively binding substrates.
ANSWER:
a)adensoine triphosphate
b) initial rate
c) serine proteases
d) transaminases
Double: What is the real-world counterpart of ATP?
Triple: In our analogy, what “functional group” is
transferred in the ping pong reaction?
Quadruple: What is the alt name for the specificity pocket?
Sh*t That Came Out of My Mouth– 40 Points
a) The other key redox coenzyme is _____________ (not NAD+ or CoQ).
b) ___________________ reactions, involving phosphate addition and
removal respectively, regulate both glycolysis and the Krebs Cycle.
c) Two external factors that limit the velocity of an enzymatic reaction are
_________ and _________.
d) _________________ of enzyme catalysis occurs when an inhibitor binds to
the active site of the enzyme.
ANSWER:
a) flavin adenine dinucleotide
b) Kinase and phosphatase
c) pH, solvent polarity, temperature, salt
concentration(s) and types, presence of
chaotropes, osmolytes
d) competitive inhibition
Double: What is FAD?
Triple: What happens when people are inactive?
Quadruple (What!?): What is the scientific name for
competitive inhibition?
Sh*t That Came Out of My Mouth– 50 Points
a) The _____________ noncovalent binding interaction is used to capture
ligand-binding entities in the “affinity capture” technique.
b) Two examples of reversible factors that control the catalytic capability of an
enzyme are: ______________, ________________
c) A zymogen is a protein that is converted from inactive to active forms by a
________________, typically protease cleavage.
d) _______________ is used to determine the sequence of a protein based on
sequential chemical reactivity.
ANSWER:
a) biotin-avidin
b) noncovalent modifications,
pH and pKa changes, [salt] changes, possibly
others
c) covalent modification
d) Edman degradation
Double: Draw and describe biotin.
Triple: What is the name of my adult club?
Quadruple: When in doubt, what do you do to get
something off the bead?
I Got 99 Upshots, But a BCH Ain’t One –
10 Points
a) Our understanding of this function (N5,N10-methylenetetrahydrofolate) can
be used in a strategy for (treatment technique)
b) The coenzyme _______________ often forms a Schiff base with the alphaamino group of a lysine residue in the enzyme.
c) Allosterism involves binding of a regulatory molecule at a site other than the
___________________
d) A/n ________________ works by amplifying an initial signal via several
linked protease cleavage reaction stages. (e.g., blood clotting)
ANSWER:
a) anticancer chemotherapy
b) pyridoxal phosphate
c) active site
d) enzyme cascade
I Got 99 Upshots, But a BCH Ain’t One –
20 Points
a) A ________________ has two charges which neutralize each other
b) A _________________ is the enzyme-substrate combination formed during
an enzyme catalysis event
c) What kind of reaction produces the reactivated enzyme?
d) When ATP used in some biochemical applications it yields AMP and
____________________
ANSWER:
a) zwitterion
b) Michaelis complex
c) nucleophilic substitution
d) pyrophosphate
I Got 99 Upshots, But a BCH Ain’t One –
30 Points
a) The heavy metal _____________ is used to facilitate the biochemical reaction in
xanthine oxidase, a key enzyme in purine catabolism.
b) List the two “binding modes of catalysis”.
c) The Arrhenius equation accounts for the temperature dependence of the
___________.
d) Two two examples of irreversible factors that control the catalytic capability of an
enzyme are: ______________, ________________
ANSWER:
a) molybdenum
b) proximity effect, transition
state stabilization
c) rate of a reaction
d) covalent modification, proteolysis, irreversible
inhibitors
I Got 99 Upshots, But a BCH Ain’t One –
40 Points
a) A common process used to produce a nucleophile is:
b) _______________ is typically required to achieve optimal activity with
(answer 46 “ATP”)-cosubstrate enzyme reactions
c) The antibiotic __________________ selectively inhibits cell wall
peptidylglycan synthesis in bacteria
d) The key polysaccharide in the liver is _________________
ANSWER:
a) acid-base catalysis
b) Mg +2
c) penicillin
d) glycogen
I Got 99 Upshots, But a BCH Ain’t One –
50 Points
DAILY
TRUFFLE