UNIT 1 - Quizzes and Exam, UNE medical biochemistry
Unit 1 Test Correctly Answered To Score A+
Which of the following amino acid would not be commonly found in the middle of
a an α-helical domain?
Proline.
It is considered a 'helix breaker' and would not be found in an alpha helix; all other
residues are nonpolar hydrophobic and could reside in a transmemebrane domain.
Changes in the physiological variables listed below can alter the affinity of
hemoglobin for oxygen. Which of the following will lower the affinity of
hemoglobin for oxygen?
a) decrease in protons
b) increase in 2,3 bisphosphoglycerate (BPG)
c) increase in pH
d) decrease in CO2
Increase in 2,3 bisphosphoglycerate (BPG)
A 22-year old female presents to the emergency department with acute abdominal
pain. She indicates the pain came on rapidly in her mid-abdominal region. She
has vomited several times over the last 4 hours. A diagnosis of acute pancreatitis
is made and she is rushed to surgery. Elevation of which of the following serum
enzymes would be consistent with this diagnosis?
Amylase
Which of the following is the best description of primary protein structure?
A newly synthesized strand of amino acids
Cleavage of fructose 1, 6-bisphosphate to dihydroxyacetone and glyceraldehyde
3-phosphate is achieved by what class of enzymes?
Lyase
Which of the following amino acid would not be commonly found in the middle of
a an α-helical domain?
Proline
Domains are common structural elements that retain a particular function within
the protein. Which of the following is an example of a protein domain?
a) a prosthetic group such as heme
b) irregular coils and loops
c) an arrangement of β-strands connected by α- helixes
d) a single α- helix
An arrangement of β-strands connected by α-helixes
α helices and β sheets are primarily stabilized by which of the following
interactions?
hydrogen bonding
Hydrogen bonding is the primary stabilizing force in both secondary structures. In alpha
,helices the hydrogen bond is between the carbonyl oxygen group from one peptide
bond and that amide hydrogen from a different peptide bond approximately amide 4
resides down in the helix. In beta sheets, the hydrogen bonding is between the carbonyl
oxygen and the amide hydrogen from different peptide strands.
Compare and contrast beta sheets and alpha helical formations. (Figure 7.3 vs. 7.5)
Phosphorylation of an amino acid changes the charge on the residue to:
Negative
The addition of a phospho group will add a large negative moiety to the amino acid and
change the functionality of the protein.
Which of the following amino acid would not be commonly found in the middle of
a an α-helical domain?
Proline
A 55-year old man is brought to the emergency room with a chief complaint of
chest pain and tingling in his left arm. Elevation of which of the following
enzymes in circulation would be most indicative of a myocardial infarction?
Troponin
A 22-year-old female is diagnosed with acute pancreatitis. Elevation of which of
the following serum enzymes would be consistent with this diagnosis?
a) lactate dehydrogenase
b) amylase
c) troponin
d) creatine kinase
amylase
Hemoglobin binds oxygen with a greater affinity in the:
R-State --- Hemoglobin binds oxygen with a greater affinity in the R state. As oxygen
binds each subunit, the affinity for oxygen increases; this is termed cooperative binding.
A 19-year-old boy is diagnosed with Creutzfeldt-Jakob Disease which is caused
by the introduction of an amyloid fold in the disease-causing protein. The
introduction of this fold causes the protein to transition from a primarily α-helical
structure to an aggregate of mostly β-sheets. This change in protein structure
(leading to disease) is best attributed to changes in which of the following?
Folding of the secondary structures
α-helices and β-sheets are primarily stabilized by which of the following
interactions
Hydrogen bonding
Movement of ammonia from an amino acid to an alpha-keto acid involves a family
of enzymes best categorized as:
a) transferases
b) ligases
c) lyases
d) isomerases
transferases
, Which of the following proteins is likely to have quaternary structure?
a) a protein that contains both α-helix and β-sheet secondary structures
b) a multimeric protein that contains multiple peptide chains
c) a small protein consisting of a single amino acid chain
d) a large transmemberane protein with seven alpha helical domains
a multimeric protein that contains multiple peptide chains
A decrease in blood pH from 7.0 to 6.0 would be accompanied by which of the
following changes in ion concentration?
A 10-fold increase in hydrogen ion concentration-
Explanation: The pH is the negative log of the hydrogen ion concentration, [H+]. At a pH
of 7.0 [H+] is 10-7; and at pH 6.0[H+] is 10-6. The [H+] has changed by a factor of 10-
6/10-7 which is 10. A decrease in 1 pH units is a 10 fold increase in [H+]
Cleavage of fructose 1, 6-bisphosphate to dihydroxyacetone and glyceraldehyde
3-phosphate is achieved by what class of enzymes?
Lyase
A 55-year old man is brought to the emergency room with a chief complaint of
chest pain and tingling in his left arm. Elevation of which of the following
enzymes in circulation would be most indicative of a myocardial infarction?
Troponin
Which of the following is the best description of primary protein structure?
A newly synthesized strand of amino acids
Discriminate between primary, secondary, tertiary, and quaternary protein structure
(Overview Figure 7.1)
Hemoglobin bound to heme is termed a holoprotein. The heme or porphyrin ring
is required for oxygen binding and it is defined as which of the following?
Prosthetic group
An enzyme has a mutation within the substrate binding site that reduces the
binding of the coenzyme needed for covalent catalysis. Which of the following is
likely to result as a consequence of this mutation?
The enzyme will not be able to form the transition state complex
Cleavage of fructose 1, 6 bisphosphate to dihydroxyacetone and glyceraldehyde
3-phosphate is achieved by what class of enzymes?
a) ligase
b) lyase
c) transferase
d) hydrolase
Lyase
Hemoglobin bound to heme is termed a holoprotein. The heme or porphyrin ring
is required for oxygen binding and it is termed a:
prosthetic group
Hemoglobin or myoglobin bound to the heme prosthetic group is termed a holoprotein.
Without the heme the protein is termed an apoprotein.
Unit 1 Test Correctly Answered To Score A+
Which of the following amino acid would not be commonly found in the middle of
a an α-helical domain?
Proline.
It is considered a 'helix breaker' and would not be found in an alpha helix; all other
residues are nonpolar hydrophobic and could reside in a transmemebrane domain.
Changes in the physiological variables listed below can alter the affinity of
hemoglobin for oxygen. Which of the following will lower the affinity of
hemoglobin for oxygen?
a) decrease in protons
b) increase in 2,3 bisphosphoglycerate (BPG)
c) increase in pH
d) decrease in CO2
Increase in 2,3 bisphosphoglycerate (BPG)
A 22-year old female presents to the emergency department with acute abdominal
pain. She indicates the pain came on rapidly in her mid-abdominal region. She
has vomited several times over the last 4 hours. A diagnosis of acute pancreatitis
is made and she is rushed to surgery. Elevation of which of the following serum
enzymes would be consistent with this diagnosis?
Amylase
Which of the following is the best description of primary protein structure?
A newly synthesized strand of amino acids
Cleavage of fructose 1, 6-bisphosphate to dihydroxyacetone and glyceraldehyde
3-phosphate is achieved by what class of enzymes?
Lyase
Which of the following amino acid would not be commonly found in the middle of
a an α-helical domain?
Proline
Domains are common structural elements that retain a particular function within
the protein. Which of the following is an example of a protein domain?
a) a prosthetic group such as heme
b) irregular coils and loops
c) an arrangement of β-strands connected by α- helixes
d) a single α- helix
An arrangement of β-strands connected by α-helixes
α helices and β sheets are primarily stabilized by which of the following
interactions?
hydrogen bonding
Hydrogen bonding is the primary stabilizing force in both secondary structures. In alpha
,helices the hydrogen bond is between the carbonyl oxygen group from one peptide
bond and that amide hydrogen from a different peptide bond approximately amide 4
resides down in the helix. In beta sheets, the hydrogen bonding is between the carbonyl
oxygen and the amide hydrogen from different peptide strands.
Compare and contrast beta sheets and alpha helical formations. (Figure 7.3 vs. 7.5)
Phosphorylation of an amino acid changes the charge on the residue to:
Negative
The addition of a phospho group will add a large negative moiety to the amino acid and
change the functionality of the protein.
Which of the following amino acid would not be commonly found in the middle of
a an α-helical domain?
Proline
A 55-year old man is brought to the emergency room with a chief complaint of
chest pain and tingling in his left arm. Elevation of which of the following
enzymes in circulation would be most indicative of a myocardial infarction?
Troponin
A 22-year-old female is diagnosed with acute pancreatitis. Elevation of which of
the following serum enzymes would be consistent with this diagnosis?
a) lactate dehydrogenase
b) amylase
c) troponin
d) creatine kinase
amylase
Hemoglobin binds oxygen with a greater affinity in the:
R-State --- Hemoglobin binds oxygen with a greater affinity in the R state. As oxygen
binds each subunit, the affinity for oxygen increases; this is termed cooperative binding.
A 19-year-old boy is diagnosed with Creutzfeldt-Jakob Disease which is caused
by the introduction of an amyloid fold in the disease-causing protein. The
introduction of this fold causes the protein to transition from a primarily α-helical
structure to an aggregate of mostly β-sheets. This change in protein structure
(leading to disease) is best attributed to changes in which of the following?
Folding of the secondary structures
α-helices and β-sheets are primarily stabilized by which of the following
interactions
Hydrogen bonding
Movement of ammonia from an amino acid to an alpha-keto acid involves a family
of enzymes best categorized as:
a) transferases
b) ligases
c) lyases
d) isomerases
transferases
, Which of the following proteins is likely to have quaternary structure?
a) a protein that contains both α-helix and β-sheet secondary structures
b) a multimeric protein that contains multiple peptide chains
c) a small protein consisting of a single amino acid chain
d) a large transmemberane protein with seven alpha helical domains
a multimeric protein that contains multiple peptide chains
A decrease in blood pH from 7.0 to 6.0 would be accompanied by which of the
following changes in ion concentration?
A 10-fold increase in hydrogen ion concentration-
Explanation: The pH is the negative log of the hydrogen ion concentration, [H+]. At a pH
of 7.0 [H+] is 10-7; and at pH 6.0[H+] is 10-6. The [H+] has changed by a factor of 10-
6/10-7 which is 10. A decrease in 1 pH units is a 10 fold increase in [H+]
Cleavage of fructose 1, 6-bisphosphate to dihydroxyacetone and glyceraldehyde
3-phosphate is achieved by what class of enzymes?
Lyase
A 55-year old man is brought to the emergency room with a chief complaint of
chest pain and tingling in his left arm. Elevation of which of the following
enzymes in circulation would be most indicative of a myocardial infarction?
Troponin
Which of the following is the best description of primary protein structure?
A newly synthesized strand of amino acids
Discriminate between primary, secondary, tertiary, and quaternary protein structure
(Overview Figure 7.1)
Hemoglobin bound to heme is termed a holoprotein. The heme or porphyrin ring
is required for oxygen binding and it is defined as which of the following?
Prosthetic group
An enzyme has a mutation within the substrate binding site that reduces the
binding of the coenzyme needed for covalent catalysis. Which of the following is
likely to result as a consequence of this mutation?
The enzyme will not be able to form the transition state complex
Cleavage of fructose 1, 6 bisphosphate to dihydroxyacetone and glyceraldehyde
3-phosphate is achieved by what class of enzymes?
a) ligase
b) lyase
c) transferase
d) hydrolase
Lyase
Hemoglobin bound to heme is termed a holoprotein. The heme or porphyrin ring
is required for oxygen binding and it is termed a:
prosthetic group
Hemoglobin or myoglobin bound to the heme prosthetic group is termed a holoprotein.
Without the heme the protein is termed an apoprotein.
