Haemoglobin (AQA Unit 2)

Unit 10, the variety of life.

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What is the primary structure of haemoglobin?
Four polypeptide chains
1 of 5
In which structure do the polypeptide chains become coiled into a helix?
The secondary structure
2 of 5
What happens to the polypeptide chains during the tertiary structure?
Each one is folded into a precise shape
3 of 5
How does haemoglobin load and unload oxygen into its structure
They change shape
4 of 5
What happens to form the quaternary strucuture?
The polypeptide chains are linked and gain a haem group
5 of 5

Other cards in this set

Card 2

Front

In which structure do the polypeptide chains become coiled into a helix?

Back

The secondary structure

Card 3

Front

What happens to the polypeptide chains during the tertiary structure?

Back

Preview of the front of card 3

Card 4

Front

How does haemoglobin load and unload oxygen into its structure

Back

Preview of the front of card 4

Card 5

Front

What happens to form the quaternary strucuture?

Back

Preview of the front of card 5

Comments

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Aren't the answers to 6 and 7 wrong?

how can both 7 and 8 be 'haemoglobin with a high affinity for oxygen'

GraphicDavey B

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Yeah im pretty sure the answer to Q7 is wrong, sorry :(

Kayleigh Nicholson

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oops! I copy and pasted the answers for 7 & 8, so I forgot to change the right answer thing :P

Kayleigh Nicholson

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Thanks for pointing it out tho :)

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