7.1 Haemoglobin

Question 1

Explain the structure of haemoglobin

Answer 1

• primary structure, sequence of amino acids in the four poly peptide chains
• secondary structure, each of these polypeptide chains is coiled into a helix
• teritary structure, each polypeptide chain is folded into a precise shape (important factor in its ability to carry oxygen)

-quaternary structure, all 4 polypeptides are linked together to form an almost spherical molecule
(each polypeptide is associated with a haem group (which contains Fe 2+ ion)) (each ferrous ion can combine with a single oxygen molecule making a total of 4 02 molecules that can be carried by a single haemoglobin molecule in humans

Question 2

What is the term used to describe haemoglobin binding with oxygen?

Answer 2

Loading or associating

takes place in lungs for humans

Question 3

What is the term used for when haemoglobin release oxygen?

Answer 3

Unloading or dissociating

takes place in tissue for humans

Question 4

Define high affinity

Answer 4

strength by which 2 or more molecules interact or bind // are attracted to each other

Question 5

What is the role of haemoglobin and what properties does it have for efficient transport of o2?

Answer 5

To transport oxygen.

1. readily associate with oxygen at the surface where gas exchange takes place
2. readily dissociate from oxygen at those tissues requiring it

Question 6

Why is haemoglobin able to change affinity (chemical attraction) for 02 under different conditions?

Answer 6

Because its shape changes in the presence of certain substances e.g c02. In the presence of c02 the new shape of the haemoglobin molecule binds more loosely to oxygen. As a result haemoglobin releases its oxygen.

Question 7

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Answer 7

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