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Hemerythrin and hemocyanin are:


A) human mutant hemoglobins with decreased oxygen affinity.
B) hemoglobin variants that are found in animals at high altitude.
C) synthetic derivatives of hemoglobin's heme group used in artificial blood substitutes.
D) oxygen transport proteins found in invertebrates.
E) tetrameric hemoglobin derivatives containing only α\alpha -chains ( α\alpha 4 tetramers) .

F) A) and E)
G) C) and E)

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Consider a hypothetical hemoglobin-like molecule with a Hill coefficient (constant) of 1 and the same p50 value as normal hemoglobin.Choose the statement below that best describes the two proteins.


A) There is a cooperative interaction between oxygen-binding sites in both the hypothetical and normal hemoglobins.
B) The hypothetical hemoglobin has a greater oxygen affinity than normal hemoglobin.
C) The oxygen binding curve for the hypothetical hemoglobin is hyperbolic, and the curve for normal hemoglobin is sigmoidal.
D) The two hemoglobins would be able to deliver about the same amount of oxygen to the tissues.
E) At pO2 less than p50, normal hemoglobin has a greater YO2 value.

F) D) and E)
G) A) and B)

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Which gas does not bind to the porphyrin ring Fe(II) ion in myoglobin?


A) NO
B) CO
C) CO2
D) O2
E) H2S

F) A) and E)
G) A) and D)

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Muscle contraction is directly caused by


A) structural changes in actin.
B) structural changes in myosin.
C) structural changes in the A band.
D) structural changes in the Z disk.
E) None of the above is correct.

F) A) and B)
G) A) and D)

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Mammals and other animals have a circulatory system because diffusion is to slow to supply the tissues with oxygen in animals that are larger than 2 millimeter.Explain in one sentence why these circulatory systems contain hemoglobin or other oxygen binding proteins?

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Oxygen-binding proteins increa...

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Hemoglobin is a heterotetramer.How many protomers are present in hemoglobin?


A) 0
B) 1
C) 2
D) 3
E) 4

F) A) and B)
G) A) and C)

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Which statement about actin is not true?


A) There are two actin genes, one for F-actin and one for G-actin.
B) Monomeric G-actin polymerizes to form F-actin.
C) Actin filaments are polar (the ends can be distinguished) .
D) Actin can bind ATP.
E) Actin is a common protein in nonmuscle cells.

F) A) and D)
G) A) and C)

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The oxygen binding by hemocyanins is mediated by


A) an iron ion
B) a pair of iron ions
C) a heme group
D) a copper atom
E) a pair of copper atoms

F) B) and D)
G) A) and C)

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The Bohr effect refers to


A) the decrease in affinity of Hb for O2 when the pH goes down
B) the decrease in affinity of Hb for O2 when the pH goes up
C) the increase in the affinity of Hb for O2 when the O2 concentration goes up
D) the decrease in affinity of Hb for O2 when the BPG concentration goes up
E) the decrease in affinity of Hb for O2 when the BPG concentration goes down

F) A) and B)
G) A) and C)

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Myoglobin's secondary structure is primarily composed of ______________.


A) parallel β\beta -sheets
B) antiparallel β\beta -sheets
C) ( α\alpha -helices)
D) ( Ω\varOmega -loops)
E) polyproline helices

F) A) and C)
G) A) and E)

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If the gene for myoglobin is "knocked out" in mice, the mice:


A) have larger lungs.
B) respire extremely rapidly.
C) have dark brown muscle tissue.
D) appear normal, with lighter colored muscle tissue.
E) have their growth stunted.

F) C) and D)
G) A) and C)

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You have been studying O2 binding to a hemerythrin-like protein isolated from an exotic marine worm.Your O2-binding data are shown in the table below. a.Use the data to generate an O2-binding curve (do not forget to mark the axes). b.Use the curve to estimate the Kd for the interaction. c.Is there any evidence from your data that this hemoglobin-like protein binds O2 in a cooperative manner (briefly explain your answer)? You have been studying O<sub>2</sub> binding to a hemerythrin-like protein isolated from an exotic marine worm.Your O<sub>2</sub>-binding data are shown in the table below. a.Use the data to generate an O<sub>2</sub>-binding curve (do not forget to mark the axes). b.Use the curve to estimate the K<sub>d</sub> for the interaction. c.Is there any evidence from your data that this hemoglobin-like protein binds O<sub>2</sub> in a cooperative manner (briefly explain your answer)?     You have been studying O<sub>2</sub> binding to a hemerythrin-like protein isolated from an exotic marine worm.Your O<sub>2</sub>-binding data are shown in the table below. a.Use the data to generate an O<sub>2</sub>-binding curve (do not forget to mark the axes). b.Use the curve to estimate the K<sub>d</sub> for the interaction. c.Is there any evidence from your data that this hemoglobin-like protein binds O<sub>2</sub> in a cooperative manner (briefly explain your answer)?

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a.see curve blured image
b.see curve, Kd e...

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Matching -Mutations that favor the oxidation of the heme iron(II) to iron(III) can cause ______.


A) positively cooperative
B) cyanosis
C) His E7
D) decrease
E) R
F) hydrogen bonds
G) increase
H) symmetry
I) His F8
J) ion pairs
K) T
L) hemolytic anemia
M) sequencial

N) E) and K)
O) C) and K)

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Myoglobin's primary physiological role is to facilitate oxygen ________.


A) storage
B) metabolism
C) binding
D) reduction
E) diffusion

F) B) and E)
G) A) and E)

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