Haemoglobin and Myoglobin Flashcards

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1
Q

What are the key features of the structure of haemoglobin?

A

2 polypetide chains, alpha (141 amino acids) and beta (146 amino acids) in a tetramer of two alpha chains and two beta chains. Confirmation of each polypeptide chain is similar to myoglobin .

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2
Q

What are the two oxygen binding states of haemoglobin?

A

T state=low affiniity

R state= high affinity

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3
Q

How does binding of oxygen increase the affinity of a globin molecule for oxygen?

A

Fe in deoxyhaemoglobin is slightly below the plane of the ring, binding of a oxygen helps to pull the fe into the plane of the ring and therefore increases the binding capabilities for oxygen.

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4
Q

What kind of binding curve does haemoglobin display?

A

Sigmodial

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5
Q

What kind of binding curve does myoglobin display?

A

Hyperbolic

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6
Q

How does 2,3 bisphosphoglycerate affect oxygen binding and how can this be beneficial?

A

2,3 bisphosphoglycerate reduces the affinity of haemoglobin to oxygen. This is useful as it is a by-product of glycolysis so oxygen can be directed to metabolically active tissues and can also be used to increase release of oxygen from haemoglobin at high altitudes.

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7
Q

What is the effect of CO2 and h+ on tissues commonly known as and what is the benefit of this?

A

This is called the Bohr affect, and this is a decrease in the affintiy of heamoglobin for oxygen in the presence of these substances. It means that more oxygen can be delivered for metabollically active tissues.

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8
Q

What is the mutation present in sickle cell anaemia and how des this affect protein structure?

A

This is a mutation from glutamate to valine in the beta-globin chain, which forms a sticky hydrophobic pocket that allows oxygenated hameoglobin to polymerise, making cells more prone to lyse and a lower flexibility of blood molecules.

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9
Q

What is a thalassemnia?

A

A group of genetic disorders resulting from a imbalance between the alpha and beta globin chains?

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10
Q

What is the effect of b-thalassemia?

A

There is decreased or absent b-chain production, resulting in a chains being unable to form stable tetramers. This is a condition which typically onsets after birth.

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11
Q

What is the effect of a-thalassemia?

A

There are varying levels of severity due to the presence of multiple genes from the alpha chains, however, beta chains can form stable tetramers with increased affinity for oxygen.

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12
Q

What are the key features of myoglobin structure

A

75% a helical, 153 amino acids, compact, histidine 93 in 8th alpha helix is covalently linked to fe.

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