how haemoglobin acts as an allosteric protein?
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Answer / pallavi kushwaha
Allosteric proteins are the protein whose shape is changed
when it binds to a particular molecule and in it's new
shape the protein ability to react a second molecule also
changed.In case of hemoglobin, in deoxyhemoglobin the
globin molecule are tightly bound in tense(T)
configurationand having very less affinity for oxygen. When
oxygen is first bound, configuration of hemoglobin
changed,bond holding the globin units are
released,producing a relaxed(R) configuration which exposes
more oxygen binding site.thus it acts as allosteric
protein, this interactive binding phenomenon is also termed
cooperativity.
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Answer / krishnam
Haemoglobin is anallosteric protein.
the binding of o2 to haemoglobin enhances the binding of
extra o2 to hte same haemoglobin molecule.oxygen binds
cooperatively to haemoglobin.
The affinity of haemoglobin for o2 depends on ph.
oxygen affinity of haemoglobin is further regulated by
organic phosphates such as 2,3-biphosphoglycerate.
because of all these reasons haemoglobin acts as an
allosteric protein.
Is This Answer Correct ? | 6 Yes | 3 No |
Answer / r.rajani
Haemoglobin is anallosteric protein.The binding of o2 to
haemoglobin enhances the binding of extra o2 to hte same
haemoglobin molecule.oxygen binds cooperatively to
haemoglobin.The affinity of haemoglobin for o2 depends on ph.
oxygen affinity of haemoglobin is further regulated by
organic phosphates such as 2,3-biphosphoglycerate.
because of all these reasons haemoglobin acts as an
allosteric protein.
Is This Answer Correct ? | 6 Yes | 3 No |
Answer / ammuz
Hemoglobin (Hb) is allosteric. An allosteric protein is
protein that has cooperative interactions between binding
sites. In Hb the binding of an O2 molecule to one site
triggers a conformational change in the molecule that sort
of "opens up" other sites, allowing for more O2 to bind.
Thus, the binding of one O2 molecule cooperatively allows
for the binding of another
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Answer / b. adhikary
when hemoglobin binds to o2 it enhance the binding more o2
into it. but when hemoglobin is reached more o2 binding
then it inhibited by product feed back inhibition.
Is This Answer Correct ? | 0 Yes | 1 No |
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