Heamoglobin

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  • Created by: Jenna k
  • Created on: 27-03-14 19:15
What is the structure of an amino acid?
There is a amino group, consisting of NH2. There is a carboxyl group, consisting of COOH, and finally the R group, which is the variable group, consisting of CH and a variation R.
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What is the primary sturcture of a protein?
A chain of amino acids joined by peptide bonds.
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What is the secondary structure of a protein?
This is when two chains of polypeptides form a helix structure due to the hydrogen bonds between the NH and the C=O group.
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What is the tertiary structure of a protein?
The alpha helix of the secondary structure is twisted and folded even further. More bonds form (Disulfide, ionic and hydrogen bonds) creating a 3D structure.
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What is the Quaternary structure of a protein?
This is where an number of tersiary structures are bonded to creat a larg mad of protein.
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How is a polypeptide bond formed?
A condensation reaction occurs between the NH and the C=OH section of the amino acid.
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How is heamoglobin different to the quaternary structue of protein?
It has a mixture of alpha and beta chains and it has a heam group.
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What does Heamoglobin stand for?
Heam is a structure that has a afinity for oxygen. The globin is a mixture of alpha and beta polypeptide chains that creat an extensive 3D structure.
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What is the role of heamoglobin?
To transport oxygen to the tissues.
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What is loading?
Loading is the process of oxygen binding with the iron molecules of the heam group.
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What is unloading?
This is the process where by oxygen is released into tissues that have a lower concentration of oxygen. Therefore theoxygne diffused into the tissues form the blood stream.
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What makes heamoglobin efficient?
It has a high affinity for oxygen, it loads readily and disociated form oxygen readily too.
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What is used to show movement of oxygen via heamogobin?
Oxygen Dissociation curve.
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Draw a ODC for a human.
.
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Whats the main difficault for heamoglobin?
Trying to bind with the first oxygen is difficult but after that it goes quite quickly.
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If an organism is less active which way would the ODC move?
To the left
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If an organism is more active which was would the OSC move?
To the right
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What is the effect of carbon dioxide on heamoglobin?
Heamoglobin has a reduced affinity for oxygen in the presents of CO2. Thus oxygen is inloaded more readily.
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Explain the process on Oxygen transportation by heamoglobin.
Lungs -High affinity load more readily. Move to tissues through blood vessels. Tissues - Presents of CO2 due to respirtaion cause Lower affinity, Unload more readily. Transport back to lungs.
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What affects Heamoglobin
pH, CO2
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Why does CO2 cause disociation?
CO2 is low in pH which changes the shape of the heamoglobin thus changing its function, and it realeases the oxygen. However it return to its shape when in normal pH's.
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Card 2

Front

What is the primary sturcture of a protein?

Back

A chain of amino acids joined by peptide bonds.

Card 3

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What is the secondary structure of a protein?

Back

Preview of the front of card 3

Card 4

Front

What is the tertiary structure of a protein?

Back

Preview of the front of card 4

Card 5

Front

What is the Quaternary structure of a protein?

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