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Biology AQA unit 2 > Haemoglobin > Flashcards

Haemoglobin Flashcards

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1
Q

what protein structure is a haemoglobin molecule?

A

quaternary

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2
Q

what is the primary structure of a haemoglobin molecule?

A

four polypeptide chains

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3
Q

what is the secondary structure of haemoglobin?

A

each of the polypeptide chains are coiled into a helix

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4
Q

what is the tertiary structure of haemoglobin?

A

each polypeptide chain is folded into a precise shape- an important factor in it’s ability to carry oxygen

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5
Q

what it the quaternary structure of haemoglobin?

A

all 4 polypeptide chains are linked together to form an almost spherical molecule.
each polypeptide is associated with a haem group

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6
Q

how many oxygen molecules can be carried by one haemoglobin molecule in humans?

A

4

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7
Q

what does a single oxygen molecule combine with?

A

an Fe ion

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8
Q

what is the role of haemoglobin?

A

to transport oxygen

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9
Q

what does haemoglobin need to do?

A

readily ASSOCIATE with oxygen at the surface where gas exchange takes place

readily DISSOCIATE with oxygen at tissues requiring it

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10
Q

when does haemoglobin change its affinity for oxygen?

A

under different conditions

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11
Q

what happens to haemoglobin in the presence of carbon dioxide?

A

the haemoglobin changes shape and binds MORE LOOSLY to oxygen

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12
Q

what are the two different types of haemoglobin?

A
  • High affinity- take up o2 easily but releases less readily

* Low affinity- take up o2 less easily but releases more readily

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13
Q

what type of haemoglobin would an organism that lives in an environment with little oxygen have?

A

high affinity haemoglobin

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14
Q

what type of haemoglobin would an organism that has a high metabolism have?

A

low affinity haemoglobin

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15
Q

what changes the affinity of the haemoglobin?

A

the shape of the molecule

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16
Q

what do different haemoglobins have?

A

slightly different sequences of amino acids, so slightly different shapes

17
Q

where does associating/loading take place?

A

in the lungs

18
Q

where does dissociating/unloading take place?

A

in the tissues

19
Q

what is the Bohr effect?

A

haemoglobin’s oxygen binding affinity is inversely related both to acidity and to the concentration of carbon dioxide.

Biology AQA unit 2 (20 decks)

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