BIOC192 practice test Flashcards
1
Q
- What is the central dogma of molecular biology?
A. RNA->DNA->Protein B. Protein->RNA->DNA C. DNA->RNA->Protein D. Lactase->DNA->ATP
A
C
2
Q
- What determines the function of a protein?
A. Its 3D shape.
B. Itscolour.
C. Its cofactors.
D. Its 2D structure.
A
A
3
Q
- The sequence of what in a protein determines how it folds?
A. Bases
B. Aminoacids C. Sugars
D. phospholipids
A
B
4
Q
- Why might a biochemist make a particular protein in the laboratory?
A. To determine its function.
B. To determine its structure.
C. To determine what it interacts with.
D. All the above.
A
D
5
Q
- Proteins are polymers of:
A. nucleoside monophosphates linked together by covalent bonds.
B. amino acids linked together by ester covalent bonds.
C. amino acids linked together by peptide covalent bonds.
D. amino acids linked together by non-covalent omega bonds.
A
C
6
Q
- Which statement about the amino acid glycine is INCORRECT?
A. It is commonly part of alpha helices.
B. It provides local flexibility to a protein.
C. It is often found in turns.
D. It is not involved in disulfide bond formation.
A
A
7
Q
- Which one of the following statements about the amino acid (cysteine, at neutral pH) shown below is INCORRECT?
A. It has a side chain that can become deprotonated at high pH.
B. It can be involved in forming covalent bonds that stabilise tertiary
structures.
C. It is commonly found in beta turns connecting the strands of beta-sheets.
D. It can be involved in forming a type of post-translational modification.
A
B
8
Q
- The amino acid pictured below:
A. is classified as a charged amino acid.
B. is likely to be found in the hydrophobic core of a protein.
C. when found at the N-terminus of a protein (at physiological pH) has no
net charge.
D. has a sidechain which commonly forms hydrogen bonds that stabilise
alpha helices.
A
B
9
Q
- Which forms of the alpha-amino and alpha-carboxyl groups of alanine are most likely to occur at very high pH (for the free amino acid)?
A. NH3+ and COO- B. NH2andCOO- C. NH2 and COOH D. NH3+ and COOH
A
D
10
Q
- Which one of the following statements about the peptide bond in proteins is INCORRECT?
A. The peptide bond is planar.
B. The peptide bond is never in the cis conformation.
C. The peptide bond is rigid.
D. The peptide bond is an example of an amide bond.
A
C
11
Q
- Amino acid side chain modification such as:
A. phosphorylation is commonly used to control enzyme activity, like an ON/OFF switch.
B. hydroxylation facilitates hydrogen bond formation required for the activation of blood clotting factors.
C. carboxylation, when applied to haemoglobin, can be used to diagnose, and monitor diabetes.
D. glycosylation catalyses disulfide bond formation to stabilise tertiary protein structures.
A
A
12
Q
- What level(s) of protein structure(s) are stabilized ONLY via hydrogen bonds?
A. Primary
B. Secondary C. Tertiary
D. Quaternary
A
B
13
Q
- An alpha helix in a protein:
A. Contains 3.6 amino acids per turn and is stabilised by covalent crosslinks.
B. Contains 4 amino acids per turn and is stabilised by hydrogen bonds
between every fourth amino acid.
C. Contains 3.6 amino acids per turn, does not normally contain proline and
is often polar on one side and non-polar on the other side.
D. Contains 3.6 amino acids per turn, has the amino acid side chains facing
the inside of the helix and can vary in length.
A
C
14
Q
- Which statement about beta turns is INCORRECT?
A. They are relatively short, normally four residues in length.
B. They commonly contain proline residues.
C. They commonly contain glycine residues.
D. They connect individual polypeptides.
A
D
15
Q
- Which statement is INCORRECT?
A. Hydrogen bonding is important for stabilizing secondary structure in proteins.
B. Hydrogen bonds in alpha helices form between the carbonyl oxygen from a peptide bond and the amino hydrogen from a different peptide bond further along the polypeptide chain.
C. Hydrogen bonds between amino acid sidechains can stabilise the tertiary structure of proteins.
D. The side chains of polar amino acids are buried deep inside of a protein to stabilise its hydrophilic core.
A
D
16
Q
- Which one of the following statements about protein structure is NOT correct?
A. Domains are discrete parts of a protein structure, usually associated with a particular function.
B. Beta-sheets are stabilised by hydrogen bonds between carbonyl oxygens and amino hydrogens from amino acids that are next to each other on the same beta-strand.
C. Proteins made from three polypeptide chains show quaternary structure.
D. The primary sequence of a polypeptide determines how the protein will fold.
A
B
17
Q
- Which statement about secondary structures is CORRECT?
A. Beta sheets are pleated structures with a slight left-handed twist.
B. Alpha helices cannot have a polar and a non-polar side.
C. Parallel beta strands are connected by supersecondary structures.
D. Turns, loops and coils connect beta strands and alpha helices together.
A
D
18
Q
- EDHWVNQYSAIT is an amino acid sequence that can form an alpha helix. Which residues are involved in forming a hydrogen bond with residue N (underlined)?
A. DandA
B. W only
C. H and S
D. V and Q
A
A
19
Q
- Which one of the following statements is INCORRECT?
A. An alpha-helix is an example of secondary structure in a protein.
B. Super-secondary structure refers to many short non-helical sequences of
amino acids that associate together in a protein.
C. The tertiary structure of a polypeptide refers to the overall three-
dimensional structure of the polypeptide.
D. The quaternary structure of a protein refers to how different polypeptide
chains are arranged in a multi-subunit protein.
A
B
20
Q
- In proteins, supersecondary structures are:
A. extra-large alpha-helices and beta-sheets.
B. structural features that have more than one secondary structure (alpha-
helix, beta-sheet) element.
C. β-turns between alpha-helices.
D. always joined together by disulphide bonds between cysteine residues
from different secondary structure elements.
A
B
21
Q
- What is the main driving force in protein folding?
A. Covalent bond formation.
B. Hydrogen bond formation.
C. Hydrophobic core formation.
D. Disulfide bond formation.
A
B
22
Q
- What is the main driving force in protein folding?
A. Covalent bond formation.
B. Hydrogen bond formation.
C. Hydrophobic core formation.
D. Disulfide bond formation.
A
B
23
Q
- Which one of the following statements regarding haem iron is CORRECT?
A. In normal oxygenated haemoglobin, the iron changes permanently from Fe(II) to Fe(III).
B. Normally the iron changes permanently from Fe(II) to Fe(III) in oxygenated myoglobin, but remains as Fe(II) in oxygenated haemoglobin.
C. Fe(III) haem cannot act as a reversible carrier of oxygen in vivo.
D. Oxygen binds to haemoglobin when BPG ceases to block the haem binding
site.
A
D
24
Q
- The T-state of haemoglobin is stabilised by:
A. Binding of bisphosphoglycerate (BPG) between subunits. B. Binding of oxygen to the Fe2+ ion in the haem.
C. Protonation of globin residue side chains.
D. CO2 binding to the Fe2+ ion in the haem.
A
25
Q
- What connects allosteric control and cooperativity?
A. Both are features of myoglobin.
B. Both give rise to a sigmoidal activity curve.
C. Both occur only in multimeric proteins.
D. Both depend on a protein shifting between R- and T-states.
A
D
26
Q
- Which one of the following statements about 2,3-bisphosphoglycerate (BPG) is CORRECT?
A. BPG binds with a higher affinity to foetal haemoglobin than to adult haemoglobin.
B. BPG increases the oxygen carrying capacity of haemoglobin.
C. BPG binds allosterically to stabilise the T state of haemoglobin.
D. BPG binds to the haem Fe to facilitate oxygen release.
A
27
Q
- Hemoglobin’s ability to deliver more than 30% of its oxygen load to resting peripheral tissues after adaptation to high altitude can be explained by:
A. a decrease in BPG thereby increasing haemoglin’s affinity for oxygen more in the lungs than in peripheral tissues.
B. a decrease in BPG thereby reducing haemoglin’s affinity for oxygen more in peripheral tissues than in the lungs.
C. an increase in BPG thereby increasing haemoglin’s affinity for oxygen more in the lungs than in peripheral tissues.
D. an increase in BPG thereby reducing haemoglin’s affinity for oxygen more in peripheral tissues than in the lungs.
A
28
Q
- Haemoglobin displays a sigmoidal oxygen binding curve because:
A. the haemoglobin subunits bind oxygen independently.
B. the haem groups in haemoglobin interact directly with each other and
influence the binding of oxygen.
C. the binding of oxygen to a haemoglobin subunit can change the conformation
of that subunit, and this change then influences the conformation and oxygen
binding ability of other subunits.
D. the haemoglobin subunits are covalently bonded together, and when one
oxygen molecule binds it causes a conformational change in all of the subunits.
A
C
29
Q
- What enables enzymes to bind to substrates very selectively?
A. The 3D geometry and chemical properties of the active site
B. Post-translational modifications of the active site.
C. Enzyme cofactors.
D. Physiological substrate concentrations.
A
A
30
Q
- An enzyme catalysed reaction:
A. releases more energy than the equivalent uncatalyzed reaction.
B. has a lower activation energy than the equivalent uncatalyzed reaction.
C. can only proceed in one direction.
D. increases the rate of reaction by bringing the energy of the products closer to
the energy of reactants (substrates).
A
B