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UNE MEDICAL BIOCHEMISTRY UNIT 1 TEST WITH 100% CORRECT ANSWERS.
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- Oxford University (OX)
UNE MEDICAL BIOCHEMISTRY UNIT 1 TEST WITH 100% CORRECT ANSWERS.
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UNE MEDICAL BIOCHEMISTRY UNIT 1TEST WITH 100% CORRECT ANSWERS
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 - answer Increase in 2,3 bisphosphoglycerate (BPG)
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 - answer An arrangement of β-strands connected by α-helixes
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 - answer amylase
, 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 - answer 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 - answer a multimeric
protein that contains multiple peptide chains
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 - answer Lyase
Which of the following best describes the structure of heme?
a) a planar porphyrin ring that binds iron
b) a nicotinamide structure that is readily oxidized
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