Quiz
Chapter 7 Hemoglobin
This quiz has question types that open in the usual player.
Questions in this quiz (38)
1Hemoglobin is a
- Ared blood cell protein that transports oxygen via its four heme-bound subunits from the lungs to the tissues
- BGives blood its red color
- Callosteric protein
- DQuaternary structure
- ETertiary structure
- Fif abnormal in primary structure can lead to diseases or mutations such as sickle cell
- Gbind of oxygen is not cooperative
2Myoglobin
- Abinds oxygen in muscle cells
- Bdisplays cooperatively in oxygen binding and release
- Cis a quaternary structure
- Dcan lead to sickle cell disease if abnormalities exist in primary structure
3The ability of myoglobin and hemoglobin to bind oxygen depends on the presence of a heme group
- ATrue
- BFalse
4The heme group consist of
- Ainorganic component called protoporphyrin and a central iron ion in the ferrous form, the only form that can bind oxygen
- Borganic component called protoporphyrin and a central iron ion in the ferrous form, the only form that can bind oxygen
- Cinorganic component called protoporphyrin and a central iron ion in the ferrous form, one out of many forms that can bind oxygen
- Dorganic component called protoporphyrin and a central iron ion in the ferrous form, one out of many forms that can bind oxygen
5The iron lies in the middle of the protoporphyrin bound to three nitrogens
- ATrue
- BFalse
6Iron can from two additional bonds, at the [blank_start]fifth[blank_end] and [blank_start]sixth[blank_end] coordination sites
- Afifth
- Bsecond
- Cfourth
- Dsixth
- Ethird
- Ffifth
7The imidazole ring of a histidine called the proximal histidine is occupied by the
- AFourth coordination
- BFifth coordination
- CSixth coordination
- DSeventh coordination
8The [blank_start]sixth[blank_end] coordination site binds [blank_start]oxygen[blank_end]
- Asixth
- Boxygen
9The structure of myoglobin prevents the release of reactive oxygen species
- ATrue
- BFalse
10Superoxide is very reactive, and should it leave the heme, ferric iron (Fe3+) would result.
- ATrue
- BFalse
11Heme with Fe3+
- Adoes not bind oxygen
- Bdoes bind oxygen
12Myoglobin with iron in the Fe3+ state is called
- Ametmyoglobin.
- Bmetamyoglobin
- Coxymyoglobin
- Ddeoxymyoglobin
13The distal histidine of myoglobin prevents the release of
- AFe3+
- BO2-
- CFe
- DO2
14A hydrogen bond donated by the distal histidine residue to the bound oxygen molecule helps stabilize oxymyoglobin
- ATrue
- BFalse
15Myoglobin consist of
- Aa single polypeptide chain, formed of α- helices connected by turns, with one oxygen binding site
- Ba multiple polypeptide chains, formed of α- helices connected by turns, with one oxygen binding site
- Ca multiple polypeptide chains, formed of β- helices connected by turns, with one oxygen binding site
- Da single polypeptide chain, formed of β- helices connected by turns, with one oxygen binding site
16Hemoglobin consist of
- AFour chains
- B2 identical α chains
- C4 identical α chains
- D2 identical β chains.
- E4 identical β chains.
17Many 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
- Aglobin
18Hemoglobin binds oxygen cooperatively
- ATrue
- BFalse
19[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]
- AMyoglobin
- BHemoglobin
- Chyperbolic
- Dsigmoid
- Ehemoglobin
- Fmyoglobin
- Gsigmoid
- Hhyperbolic
- Icooperative
- Jnon-cooperative
20Hemoglobin is not effective in providing oxygen to exercising tissue
- ATrue
- BFalse
21Because of cooperatively between O2 binding sites,
- Ahemoglobin delivers more O2 to actively metabolizing tissues than would myoglobin or any noncooperative protein, even one with optimal O2 affinity
- Bhemoglobin delivers more O2 to actively metabolizing tissues than would myoglobin or any cooperative protein, even one with optimal O2 affinity
- Cmyoglobin delivers more O2 to actively metabolizing tissues than would hemoglobin or any noncooperative protein, even one with optimal O2 affinity
22The 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].
- AT state
- BR state
- CR state
- DT state
23R state
- Arelaxed state
- Btight state
- Cbinding of oxygen
- Dfacilitates the release of oxygen
24T state
- ATight state
- BRelaxed state
- Cbinding of oxygen
- Dfacilitates the release of oxygen
25R state has a greater affinity for oxygen than does the T state
- ATrue
- BFalse
26It is sequential in that in hemoglobin with one O2 bound,
- Athe remaining subunits are in the T state.
- Bthe remaining subunits are in the R state.
27It is concerted in that in hemoglobin with three O2 bound,
- Athe remaining subunit is in the R state
- Bthe remaining subunit is in the T state
28The transition from deoxyhemoglobin (T state) to oxyhemoglobin (R state) occurs upon oxygen binding.
- ATrue
- BFalse
292,3 Bisphosphoglycerate in red cells is crucial in determining the oxygen affinity of myoglobin
- ATrue
- BFalse
302, 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.
- AT state
- BR state
- Crelease
- Dbinding
312. 2, 3-BPG binds to a pocket in the hemoglobin tetramer that exists only when hemoglobin is in the R state.
- ATrue
- BFalse
32In fetal hemoglobin,
- Athe β chain is replaced with a γ chain
- BThe fetal α2γ2 hemoglobin does not bind 2, 3-BPG as well as adult hemoglobin does.
- CThe 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
33Carbon 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.
- ATrue
- BFalse
34Bohr effect
- AThe stimulation of oxygen release (R state) by carbon dioxide and Hydrogen ions
- BThe stimulation of oxygen release (T state) by carbon dioxide and Hydrogen ions
35Most carbon dioxide is carried to the lungs in the blood as bicarbonate ion.
- ATrue
- BFalse
36Carbonic acid dissociates to form HCO3- and H+ resulting in a rise in pH inside the cell
- ATrue
- BFalse
37Sickle cell anemia results from the aggregation of mutated deoxyhemoglobin molecules
- Ais a genetic disease caused by a mutation resulting in the substitution of valine for glutamate at position 6 of the β chains.
- Bcan be fatal when both alleles of the β chain are mutated.
- Ctrait offers some protection from malaria
- Done allele is mutated and one is normal such individuals are asymptomatic.
38Thalassemia
- Acaused by an imbalanced production of hemoglobin chains
- Banother common genetic disorder of hemoglobin
- Canother common genetic disorder of myoglobin
- Dcaused by the absence or underproduction of one of the hemoglobin chains
- Ecaused by the presence or overproduction of one of the hemoglobin chains
Information
- Description
- Chapter 7
- Author
- Amy Arce
- Language
- English
- Views
- 55
- Tags
- Rating
- No ratings yet Rate this quiz