Pack 8 - Mass Transport Flashcards
Describe the primary structure of haemoglobin?
Sequence of amino acids
Describe the secondary structure of haemoglobin?
Polypeptide chains are cooked into an α helix
Describe the tertiary structure of haemoglobin?
Each polypeptide chain is folded into a precise shape.
Describe the quaternary structure of haemoglobin?
Four polypeptide chains are linked to form an almost spherical molecule. Each chain is associated with a ham group which contains Fe²⁺.
How many O₂ molecules can one haemoglobin molecule combine with and why?
4 as there are 4 harm groups in one haemoglobin molecule.
Give two names for the process by which O₂ binds to haemoglobin.
Loading/associating.
Give two names for the process by which O₂ is released from haemoglobin.
Unloading/dissociating
Where does loading/association of O₂ to haemoglobin occur in humans?
In the capillaries of the lungs.
Where does unloading/dissociation of O₂ from haemoglobin occur in humans?
The capillaries in respiring tissues.
What is the difference between a haemoglobin molecule with a ‘high affinity for oxygen’ anda haemoglobin molecule with a ‘low affinity for oxygen’?
- A haemoglobin molecule with a ‘high affinity for oxygen’ takes up oxygen more easily but release it less easily.
- A haemoglobin molecule with a ‘low affinity for oxygen’ takes up oxygen less easily but release it more easily.
What is the role of haemoglobin?
To transport oxygen.
“to be efficient at transporting oxygen, haemoglobin must…” - Complete the statement (2 points) in terms of where oxygen is unloaded and is loaded.
- …readily associate with O₂ at the gas exchange surface.
* …readily dissociate from O₂ at the tissues requiring O₂.
Why is it important haemoglobin can change its infinity for O₂?
So it can readily associate with O₂ at the gas exchange surface.
AND so it readily dissociate from O₂ at the tissues requiring O₂.
Why does haemoglobin’s affinity for oxygen change at respiring tissues compared with in the lungs?
Haemoglobin changes its shape in the presence of CO₂ so that O₂ binds more loosely. There is a high conc. of CO₂ in the respiring tissues.
Why does haemoglobin need a low affinity for O₂ at respiring tissues?
So that O₂ is unloaded.
Do all organisms possess the same type of haemoglobin molecule?
No.
Why do different haemoglobin molecules have different affinities for O₂
They have slightly difference sequence of animo acids and therefore slightly different tertiary and quaternary structure.
Describe and explain the initial shape of an ODC (1st O₂).
- Increases slowly.
- Due to the shape of haemoglobin, it is difficult for the first O₂ to bind. Therefore at low O₂ PP, little O₂ binds so curve is shallow.
Define Partial pressure of a gas.
Concentration of a given gas in air
What does the term ‘positive cooperativity’ mean in terms of oxygen binding to Hb.
The affinity of haemoglobin for O₂ is increased by the binding of O₂ molecules.
Describe and explain the middle part of the shape of an ODC (2nd/3rd O₂).
- The binding of the first O₂ molecule changes the quaternary structure of haemoglobin, making it easier for the other harm groups to bind to O₂.
- Therefore a smaller increase in O₂ PP is required for the 2nd O₂ to bind than the 1st.
- Gradient steepens
Describe and explain the final part of the shape of an ODC (4th O₂).
For the 4th O₂ molecule however, although in theory it is easier for the molecule to bind, the curve flattens due to the probability of O₂ coming in contact with the ahem group being reduced due to the other 3 haem groups being occupied.
Fill in the gaps twice:
'’The further to the ____ the ODC, the _______ the affinity of haemoglobin for oxygen.”
left, lower, greater, right
- Left + Greater
* Right + Lower
How does the concentration fo CO₂ affect haemoglobin’s affinity for O₂? What is the name for this effect?
- The greater the concentration of CO₂, the lower the affinity go haemoglobin for O₂.
- Bohr effect