3671137
Pregunta 1
Pregunta
Hemoglobin is a
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red blood cell protein that transports oxygen via its four heme-bound subunits from the lungs to the tissues
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Gives blood its red color
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allosteric protein
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Quaternary structure
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Tertiary structure
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if abnormal in primary structure can lead to diseases or mutations such as sickle cell
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bind of oxygen is not cooperative
Pregunta 2
Pregunta
Myoglobin
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binds oxygen in muscle cells
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displays cooperatively in oxygen binding and release
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is a quaternary structure
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can lead to sickle cell disease if abnormalities exist in primary structure
Pregunta 3
Pregunta
The ability of myoglobin and hemoglobin to bind oxygen depends on the presence of a heme group
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- True
- False
Pregunta 4
Pregunta
The heme group consist of
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inorganic component called protoporphyrin and a central iron ion in the ferrous form, the only form that can bind oxygen
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organic component called protoporphyrin and a central iron ion in the ferrous form, the only form that can bind oxygen
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inorganic component called protoporphyrin and a central iron ion in the ferrous form, one out of many forms that can bind oxygen
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organic component called protoporphyrin and a central iron ion in the ferrous form, one out of many forms that can bind oxygen
Pregunta 5
Pregunta
The iron lies in the middle of the protoporphyrin bound to three nitrogens
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- True
- False
Pregunta 6
Pregunta
Iron can from two additional bonds, at the [blank_start]fifth[blank_end] and [blank_start]sixth[blank_end] coordination sites
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fifth
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second
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fourth
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sixth
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third
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fifth
Pregunta 7
Pregunta
The imidazole ring of a histidine called the proximal histidine is occupied by the
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Fourth coordination
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Fifth coordination
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Sixth coordination
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Seventh coordination
Pregunta 8
Pregunta
The [blank_start]sixth[blank_end] coordination site binds [blank_start]oxygen[blank_end]
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sixth
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oxygen
Pregunta 9
Pregunta
The structure of myoglobin prevents the release of reactive oxygen species
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- True
- False
Pregunta 10
Pregunta
Superoxide is very reactive, and should it leave the heme, ferric iron (Fe3+) would result.
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- True
- False
Pregunta 11
Pregunta
Heme with Fe3+
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does not bind oxygen
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does bind oxygen
Pregunta 12
Pregunta
Myoglobin with iron in the Fe3+ state is called
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metmyoglobin.
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metamyoglobin
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oxymyoglobin
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deoxymyoglobin
Pregunta 13
Pregunta
The distal histidine of myoglobin prevents the release of
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Fe3+
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O2-
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Fe
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O2
Pregunta 14
Pregunta
A hydrogen bond donated by the distal histidine residue to the bound oxygen molecule helps stabilize oxymyoglobin
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- True
- False
Pregunta 15
Pregunta
Myoglobin consist of
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a single polypeptide chain, formed of α- helices connected by turns, with one oxygen binding site
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a multiple polypeptide chains, formed of α- helices connected by turns, with one oxygen binding site
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a multiple polypeptide chains, formed of β- helices connected by turns, with one oxygen binding site
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a single polypeptide chain, formed of β- helices connected by turns, with one oxygen binding site
Pregunta 16
Pregunta
Hemoglobin consist of
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Four chains
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2 identical α chains
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4 identical α chains
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2 identical β chains.
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4 identical β chains.
Pregunta 17
Pregunta
Many of the helices in each subunit are arranged in a pattern also found in myoglobin, a structure called the [blank_start]globin[blank_end] fold
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globin
Pregunta 18
Pregunta
Hemoglobin binds oxygen cooperatively
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- True
- False
Pregunta 19
Pregunta
[blank_start]Myoglobin[blank_end] displays a [blank_start]hyperbolic[blank_end] oxygen binding curve, while [blank_start]hemoglobin[blank_end] exhibits a [blank_start]sigmoid[blank_end] curve, indication that O2 binding and release is [blank_start]cooperative[blank_end]
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Myoglobin
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Hemoglobin
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hyperbolic
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sigmoid
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hemoglobin
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myoglobin
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sigmoid
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hyperbolic
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cooperative
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non-cooperative
Pregunta 20
Pregunta
Hemoglobin is not effective in providing oxygen to exercising tissue
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- True
- False
Pregunta 21
Pregunta
Because of cooperatively between O2 binding sites,
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hemoglobin delivers more O2 to actively metabolizing tissues than would myoglobin or any noncooperative protein, even one with optimal O2 affinity
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hemoglobin delivers more O2 to actively metabolizing tissues than would myoglobin or any cooperative protein, even one with optimal O2 affinity
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myoglobin delivers more O2 to actively metabolizing tissues than would hemoglobin or any noncooperative protein, even one with optimal O2 affinity
Pregunta 22
Pregunta
The quaternary structure of deoxyhemoglobin is referred to as the [blank_start]T state[blank_end], while that of oxyhemoglobin is the [blank_start]R state[blank_end].
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T state
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R state
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R state
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T state
Pregunta 23
Pregunta
R state
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relaxed state
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tight state
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binding of oxygen
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facilitates the release of oxygen
Pregunta 24
Pregunta
T state
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Tight state
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Relaxed state
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binding of oxygen
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facilitates the release of oxygen
Pregunta 25
Pregunta
R state has a greater affinity for oxygen than does the T state
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- True
- False
Pregunta 26
Pregunta
It is sequential in that in hemoglobin with one O2 bound,
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the remaining subunits are in the T state.
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the remaining subunits are in the R state.
Pregunta 27
Pregunta
It is concerted in that in hemoglobin with three O2 bound,
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the remaining subunit is in the R state
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the remaining subunit is in the T state
Pregunta 28
Pregunta
The transition from deoxyhemoglobin (T state) to oxyhemoglobin (R state) occurs upon oxygen binding.
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- True
- False
Pregunta 29
Pregunta
2,3 Bisphosphoglycerate in red cells is crucial in determining the oxygen affinity of myoglobin
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- True
- False
Pregunta 30
Pregunta
2, 3-Bisphosphoglycerate (2,3-BPG) stabilizes the [blank_start]T state[blank_end] of hemoglobin and thus facilitates the [blank_start]release[blank_end] of oxygen.
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T state
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R state
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release
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binding
Pregunta 31
Pregunta
2. 2, 3-BPG binds to a pocket in the hemoglobin tetramer that exists only when hemoglobin is in the R state.
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- True
- False
Pregunta 32
Pregunta
In fetal hemoglobin,
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the β chain is replaced with a γ chain
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The fetal α2γ2 hemoglobin does not bind 2, 3-BPG as well as adult hemoglobin does.
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The reduced affinity for 2, 3-BPG results in fetal hemoglobin having a higher affinity for oxygen, binding oxygen when the mother’s hemoglobin is releasing oxygen
Pregunta 33
Pregunta
Carbon monoxide binds so tightly to iron of hemoglobin that it stabilizes the R state (binding of oxygen) to such a degree that the R to T transition does not occur.
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- True
- False
Pregunta 34
Pregunta
Bohr effect
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The stimulation of oxygen release (R state) by carbon dioxide and Hydrogen ions
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The stimulation of oxygen release (T state) by carbon dioxide and Hydrogen ions
Pregunta 35
Pregunta
Most carbon dioxide is carried to the lungs in the blood as bicarbonate ion.
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- True
- False
Pregunta 36
Pregunta
Carbonic acid dissociates to form HCO3- and H+ resulting in a rise in pH inside the cell
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- True
- False
Pregunta 37
Pregunta
Sickle cell anemia results from the aggregation of mutated deoxyhemoglobin molecules
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is a genetic disease caused by a mutation resulting in the substitution of valine for glutamate at position 6 of the β chains.
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can be fatal when both alleles of the β chain are mutated.
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trait offers some protection from malaria
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one allele is mutated and one is normal such individuals are asymptomatic.
Pregunta 38
Pregunta
Thalassemia
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caused by an imbalanced production of hemoglobin chains
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another common genetic disorder of hemoglobin
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another common genetic disorder of myoglobin
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caused by the absence or underproduction of one of the hemoglobin chains
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caused by the presence or overproduction of one of the hemoglobin chains
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