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 -chains ( 4 tetramers) .
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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.
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A) NO
B) CO
C) CO2
D) O2
E) H2S
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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.
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A) 0
B) 1
C) 2
D) 3
E) 4
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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.
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A) an iron ion
B) a pair of iron ions
C) a heme group
D) a copper atom
E) a pair of copper atoms
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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
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A) parallel -sheets
B) antiparallel -sheets
C) ( -helices)
D) ( -loops)
E) polyproline helices
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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.
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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
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A) storage
B) metabolism
C) binding
D) reduction
E) diffusion
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