Biochemistry, Final Exam Review
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Biochemistry, Final Exam Review
Single Jeopardy Answers
Tools
Pts Answer
Question
50
This method uses a graph of log MW vs. relative
mobility to determine the apparent MW of a
protein sample.
100 This equation is used in UV absorption
spectroscopy to determine the concentration of
DNA in solution.
150 This method is used to determine the precise mass
of a protein molecule.
200 This experimental method generates specific
What is site-directed mutagenesis?
missense mutations in polypeptide chains for the
purpose of testing the functional or structural role
of a specific amino acid side chain.
250 This experimental method determines the precise What is protein footprinting?
binding site of protein on its nucleic acid ligand.
Cofactors and Coenzymes
Pts Answer
50
This metal ion is required for the protease activity
of carboxypeptidase.
100 This coenzyme serves as a methyl donor for a
variety of enzymes.
150 This vitamin is a monomeric precursor of the
photoreactive pigment in rhodopsin.
200 This organic molecule in hemoglobin contains a
protoporphyrin ring with Fe(II) in either the high
or low spin state.
250 In the dark, this coenzyme serves as the
photoreactive center of rhodopsin.
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Question
What is Zn2+?
What is coenzyme A?
What is vitamin A?
What is heme?
What is 11-cis-retinal?
3/7/16
Biochemistry, Final Exam Review
Protein Function
Pts Answer
50
This is a specific term for an antibody elicited
against a transition state analog.
100 The major function of this protein is to transport
oxygen in mammalian red blood cells.
150 This protein catalyzes the hydrolytic cleavage of
RNA molecules on the 3’ side of pyrimidine
residues.
200 This general type of enzyme catalyzes the transfer
of a phosphoryl group to a serine, threonine or
tyrosine side chain in a protein substrate.
250 This general type of enzyme catalyzes the
hydrolytic release of inorganic phosphate from a
protein substrate.
4. Experimental Results
Pts Answer
50
This type of curve provides evidence for the noncooperative oxygen binding of myoglobin.
100 The use of this chemical provides evidence of the
importance of quaternary structure for the
allosteric behaviour of hemoglobin.
150 This experimental value is equal to the partial
pressure of oxygen under conditions in which 1/2
of the myoglobin molecules in solution are
saturated with oxygen.
200 This type of curve provides evidence of the
cooperative binding of hemoglobin.
250 This type of plot gives a direct numerical measure
of the degree of cooperativity from its maximum
slope.
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Question
What is Abzyme?
What is hemoglobin?
What is ribonuclease A?
What is protein kinase?
What is phosphatase?
Question
3/7/16
Biochemistry, Final Exam Review
5. Amino Acids
Pts Answer
50
This amino acid is the bulkiest of the hydrophobic
residues.
100 This amino acid exists as a charged and
uncharged species at physiological pH.
150 This polar amino acid bears a close chemical
similarity to phenylalanine.
200 This amino acid is the smallest of the acidic
residues.
250 At physiological pH, this residue is an analog of
guanidinium.
6. Ribosomes
Pts Answer
50
This molecule serves as the template for protein
synthesis catalyzed by the ribosome.
100 Each decoding event in the A site of the
eubacterial ribosome requires this portion of the
mRNA template.
150 Peptidyl transferase activity is contained in this
component of the eubacterial ribosome.
200 This component of the eubacterial 30S ribosome
subunit is involved in selecting the initiation
region of the mRNA.
250 This hypothesis is a working model for the
nucleotide interactions that occur during decoding
in the ribosomal A site.
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Question
What is tryptophan?
What is histidine?
What is tyrosine?
What is aspartic acid?
What is arginine?
Question
What is mRNA?
What is a codon?
What is 23S rRNA in the 50S
ribosome subunit?
What is the 3’ end or anti Shine
Dalgarno region of 16S rRNA?
What is the wobble hypothesis?
3/7/16
Biochemistry, Final Exam Review
Double Jeopardy Answers
1. Proteins
Pts Answer
100 This type of amino acid isomer is generally found
in proteins on earth.
200 This type of chemical bond forms the linkage
between each residue in the polypeptide
backbone.
300 This type of protein secondary structure can fit
into the major helix of B form DNA.
400 This general feature of protein structure is found
in oligomeric but not monomeric proteins.
500 This term is used to define the pH of an aqueous
solution at which a protein has a net charge of
zero; this normally defines pH at which the
protein is most insoluble.
2. Enzyme Kinetics
Pts Answer
100 It is thought that enzymes accelerate chemical
reaction rates as a result of lowering this type of
barrier.
200 This Michaelis Menten parameter is defined as
the number of substrate molecules converted to
product per second when the enzyme is saturated
with substrate.
300 This Michaelis Menten parameter is defined as
1/2 of the maximal reaction velocity.
400 An enzyme is called perfect when the ratio of
these two parameters is equivalent to the rate of
diffusion of substrate into the active site.
500 This type of inhibitor increases the Km but has no
effect on the Vmax of the reaction catalyzed.
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Question
What is the L-isomer?
What is peptide bond?
What is the alpha helix?
What is quaternary structure?
What is the isoelectric pH?
Question
What is transition state energy or
activation energy?
What is kcat?
What is Km?
What is kcat/Km?
What is competitive inhibitor?
3/7/16
Biochemistry, Final Exam Review
3. tRNAs
Pts Answer
100 This sequence is at the end of every uncharged,
mature tRNA.
200 The amino acid of any charged tRNA is
chemically attached to this stem of the tRNA.
300 This chemical bond joins the amino acid and the
charged tRNA.
400 These enzymes attach a specific amino acid to its
cognate tRNA in the presence of ATP.
500 This molecule serves as an adaptor for the
translation of the mRNA open reading frame into
a polypeptide sequence.
4. Antibiotics
Pts Answer
100 This antibiotic is lethal to some bacteria because
it serves as a suicide inhibitor of enzymes
involved in cell wall biosynthesis.
200 This protein toxin can be lethal to humans
because it catalyzes ADP-ribosylation of
elongation factor 2.
300 This antibiotic is used to treat some antibiotic
resistant bacterial strains because it is a suicide
inhibitor of beta-lactamase.
400 This antibiotic is an analog of aminoacyl tRNA,
which induces premature release of the nascent
polypeptide chain.
500 Low levels of this antibiotic in eubacteria induce
miscoding of protein synthesis.
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Question
What is CCA?
What is amino acid acceptor stem?
What is the aminoacyl bond?
What are the amino acyl
tRNAsynthetases?
What is a charged tRNA?
Question
What is penicillin?
What is Diphtheria toxin?
What is clavulanic acid?
What is puromycin?
What is streptomycin?
3/7/16
Biochemistry, Final Exam Review
5. Enzymes - Catalysis
Pts Answer
100 This is the term used to describe the change in
enzyme conformation upon substrate binding.
200 This is the name of the cleft or surface of an
enzyme where the substrate is transformed into
product.
300 This thermodynamic parameter describes the
affinity of a Michaelis Menten enzyme for its
substrate.
400 This kinetic parameter is thought to describe the
catalytic power of an enzyme.
500 Enzymes catalyze chemical reactions in the
forward direction when the reaction exhibits this
numerical change in Gibbs free energy.
6. Ribozymes
Pts Answer
100 This metal ion is generally required for substrate
binding and/or catalytic activity of ribozymes.
200 Ribozyme activity is highly sensitive to treatment
with this chemical denaturant.
300 This catalytic activity of the ribosome is known to
be RNA based.
400 This type of chemical reaction is catalyzed by
ribonuclease P.
500 This mode of ribozyme-substrate recognition is
directed by Watson Crick base pairing.
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Question
What is Induced fit?
What is active site?
What is Ks?
What is kcat?
What is less than zero; negative?
Question
What is Mg2+?
What is urea?
What is peptidyl transferase
activity?
What is hydrolysis of the 5’
extension of pre-tRNA?
What is template recognition?
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