Brookwood Invitational Science Olympiad Tournament
Protein Modeling Exam
1) All of the following contain amino acids except
A) hemoglobin.
B) cholesterol.
C) antibodies.
Team: _______________________________
D) enzymes.
E) insulin.
2) The bonding of two amino acid molecules to form a larger molecule requires
A) the release of a water molecule.
B) the release of a carbon dioxide molecule.
C) the addition of a nitrogen atom.
D) the addition of a water molecule.
E) both B and C
3) There are 20 different amino acids. What makes one amino acid different from another?
A) different carboxyl groups attached to an alpha carbon
B) different amino groups attached to an alpha carbon
C) different side chains (R groups) attached to an alpha carbon
D) different alpha carbons
E) different asymmetric carbons
Figure 1
4) Which of the following statements is/are true regarding the chemical reaction illustrated in Figure 1?
A) It is a hydrolysis reaction.
B) It results in a peptide bond.
C) It joins two fatty acids together.
D) A and B only
E) A, B, and C
5) What is the major stabilizing force for the secondary structure of a protein?
A) peptide bonds
B) hydrogen bonds
C) disulfide bonds
D) ionic bonds
6) Which of the following describes the events of apoptosis?
A) The cell dies, it is lysed, its organelles are phagocytized, its contents are recycled.
B) Its DNA and organelles become fragmented, it dies, and it is phagocytized.
C) The cell dies and the presence of its fragmented contents stimulates nearby cells to divide.
D) Its DNA and organelles are fragmented, the cell shrinks and forms blebs, and the cell self-digests.
E) Its nucleus and organelles are lysed, the cell enlarges and bursts.
7) The alpha helix and the beta pleated sheet are both common polypeptide forms found in which level of protein
structure?
A) primary
B) secondary
C) tertiary
D) quaternary
E) all of the above
8) A strong covalent bond between amino acids that functions in maintaining a polypeptide's specific threedimensional shape is a (an)
A) hydrogen bond.
B) ionic bond.
C) van der Waals interaction.
D) disulfide bond.
Refer to Figure 2 to answer the questions 9-11.
Figure 2
9) Which bond is a peptide bond? D
10) Which bond is closest to the N-terminus of the molecule? A
11) Which bond is closest to the carboxyl end of the molecule? E
Figure 3
12) The structure depicted in the Figure on the left shows the
A) 1-4 linkage of the  glucose monomers of starch.
B) 1-4 linkage of the  glucose monomers of cellulose.
C) double helical structure of a DNA molecule.
D)  helix secondary structure of a polypeptide.
E)  pleated sheet secondary structure of a polypeptide.
13) The figure on the left best illustrates the
A) secondary structure of a polypeptide.
B) tertiary structure of a polypeptide.
C) quaternary structure of a protein.
D) double helix structure of DNA.
E) primary structure of a polysaccharide.
14) The tertiary structure of a protein is the
A) bonding together of several polypeptide chains by weak bonds.
B) order in which amino acids are joined in a polypeptide chain.
C) unique three-dimensional shape of the fully folded polypeptide.
D) organization of a polypeptide chain into an alpha helix or beta pleated sheet.
E) overall protein structure resulting from the aggregation of two or more polypeptide subunits.
15) Misfolding of polypeptides is a serious problem in cells. Which of the following diseases are associated with an
accumulation of misfolded proteins?
A) Alzheimer's
B) Parkinson's
C) diabetes
D) A and B only E) A, B, and C
16) Altering which of the following levels of structural organization could change the function of a protein?
A) primary
B) secondary
C) tertiary
D) quaternary
E) all of the above
17) The function of each protein is a consequence of its specific shape. What is the term used for a change in a
protein's three-dimensional shape or conformation due to disruption of hydrogen bonds, disulfide bridges, or
ionic bonds?
A) hydrolysis
B) stabilization
C) destabilization
D) renaturation
E) denaturation
18) What would be an unexpected consequence of changing one amino acid in a protein consisting of 325 amino
acids?
A) The primary structure of the protein would be changed.
B) The tertiary structure of the protein might be changed.
C) The biological activity or function of the protein might be altered.
D) Only A and C are correct.
E) A, B, and C are correct.
19) Why has C. elegans proven to be a useful model for understanding apoptosis?
A) The animal has very few genes, so that finding those responsible is easier than in a more complex organism.
B) The nematode undergoes a fixed and easy-to-visualize number of apoptotic events during its normal
development.
C) This plant has a long-studied aging mechanism that has made understanding its death just a last stage.
D) While the organism ages, its cells die progressively until the whole organism is dead.
E) All of its genes are constantly being expressed so all of its proteins are available from each cell.
20). Which of the following bonds is the strongest?
A. Hydrogen bond
B. Covalent bond
C. Ionic bond
D. Electrostatic bond
21). Beta sheets represent which level of protein structure?
A. Primary
B. Secondary
C. Tertiary
D. Quarternary
22). Which class of amino acids will most likely be located on the surface of a protein that is embedded within the
phospholipid cell membrane?
A. Hydrophobic amino acids
B. Hydrophilic amino acids
C. Basic amino acids
D. Acidic amino acids
23.) Human caspases can be activated by
A) irreparable DNA damage or protein misfolding.
B) infrequency of cell division.
C) high concentrations of vitamin C.
D) a death-signaling ligand being removed from its receptor.
E) electron transport.
24. Which of the following amino acids is a non‐polar amino acid?
A. Arginine
B. Lysine
C. Leucine
D. Glutamic Acid
25. How many carbon atoms are found in the backbone of each amino acid?
A. 1
B. 2
C. 3
D. 4
Onsite Build
The workstation should have the On‐Site Model Competition Environment open on the computer. Using the using
3 pipe cleaners provided, construct a model of amino acids 256-296 of 1G73Ca. The scale should be 2 cm per
amino acid. A meter stick/ruler has been provided for you. Your model of amino acids 256-296 of 1G73Ca of
should include the following:
A: Two amino acids: Indicate Arg 268 and Tyr 290 with paper clips
B: Paper clip indicating the carboxylic acid terminus (C‐terminal end) of this region of the protein