Mass Transport Flashcards
Describe the quaternary structure of haemoglobin.
Four polypeptide chains linked together by hydrogen bonds to form a spherical molecule, each polypeptide chain is associated with a haem group which aids in the co-operative binding of oxygen by serving as the binding sites for oxygen.
How many oxygen molecules can haemoglobin molecule carry?
Four O2 molecules where each O2 molecule binds to a haem group (Fe2+).
Describe the primary structure of haemoglobin, and what does this determine?
4 sequences of amino acids, which determines the proteins function and properties.
Describe the secondary structure of haemoglobin, and what does this contribute to?
Amino acid sequence coiled into a helix or pleat held together by hydrogen bonds, which contributes to the overall shape of the protein.
Describe the tertiary structure of haemoglobin, and how the formation aids in its function.
Each helix or pleat is folded into a specific shape (held together by hydrogen bonds, ionic bonds and disulphide bridges) which is crucial for its function in oxygen transport.
Describe how O2 concentration, CO2 concentration and affinity of oxygen would be affected in:
- gas exchange surfaces
- respiring tissues
- Gas exchange surfaces - high O2 concentration, low CO2 concentration, high oxygen affinity.
- Respiring tissues - low O2 concentration, high CO2 concentration, low oxygen affinity.
What is the process called when haemoglobin binds with oxygen, and where does it occur?
Loading/Associating, occurs in the lungs.
What is the process called when haemoglobin releases its oxygen and where does it occur?
Unloading/Dis-associating, occurs in the tissues where oxygen is needed.
Define Affinity.
Describe the difference between high affinity and low affinity haemoglobin.
Affinity - the strength by which two or more molecule interact or bind.
High affinity haemoglobin is adapted for efficient oxygen uptake (releasing it less easily), while low affinity haemoglobin is adapted for efficient oxygen release (up taking it less easily).
What factors about haemoglobin may make it have a different affinity for oxygen?
- different shape of haemoglobin.
- different sequence of amino acids.
What is the primary role of haemoglobin?
How can it do this efficiently in different circumstances (e.g: gas exchange surfaces vs respiring tissues)
To transport oxygen.
Efficient transport requires:
- the haemoglobin to readily associate with oxygen at gas exchange surfaces which allows for efficient uptake in the lungs.
- the haemoglobin to readily disassociate with oxygen at respiring tissues which allows for efficient release/delivery of oxygen in the cells that need it.
Define haemoglobin.
- A group of chemically similar molecules found in a wide variety of organisms.
- Protein molecules with a quaternary structure that has evolved to make it efficient at carrying O2.
What is PO2?
The partial pressure of oxygen (e.g: the ‘concentration of oxygen’)
Describe how the curve shifting can affect the oxygen affinity in haemoglobin on an oxygen dissociation curve.
- A curve shifting further to the left of the graph means a greater affinity for oxygen.
- A curve shifting further to the right of the graph means a lower affinity for oxygen.
Describe the Bohr effect (give the equation)
Explain the effect of it.
How carbon dioxide concentration affects an oxygen dissociation curve.
CO2 + H20 <==> H+ + HC03-
-Higher carbon dioxide concentration would decrease haemoglobin affinity for oxygen.
-Lower carbon dioxide concentration would increase haemoglobin affinity for oxygen.
How does the Bohr effect explain the behaviour of haemoglobin:
- in the lungs?
- in the muscles?
- Low CO2 concentration as it’s been excreted therefore higher affinity for oxygen as oxygen being loaded.
- High CO2 concentration as it’s being produced in the muscles therefore lower affinity for oxygen as oxygen being unloaded due to higher demand. (haemoglobin changes shape to reduce affinity)