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Haemoglobin Research Paper

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Describe how haemoglobin binds and releases oxygen, emphasising the role of cooperativity.
In this essay I will be describing how haemoglobins ability to change its structure between tense and relaxed form gives it the ability to change its affinity for binding and releasing oxygen, and how this regulation, cooperativity, enables the protein to carry out its function of transporting oxygen from the lungs to respiring tissues efficiently.
The structure of haemoglobin consists of 4 polypeptide chains, 2 alpha chains 141 amino acids in length and 2 beta chains 146 amino acids in length which, are both structurally similar (diatronic). Attached to each chain is a haem group which involves Fe2+ ion held in a heterocyclic ring known as porphyrin(bristol). Iron in haem is bound to 4 nitrogen atoms in the centre of the ring, leaving two binding sites, one site is occupied by a polar histidine which leaves the last site available for binding with oxygen (bristol). Haem is a prosthetic group as it is bound firmly within the active centre of the medium that it can leave the protein (book).
Haemoglobin has the ability to change shape based on the environmental conditions and comes in two structures, relaxed and tense. The difference between these two structures is a 15 degree rotation between the alpha and beta dimers (davidson). This rotation changes the …show more content…
A mutation in the DNA codes for a valine amino acid in place of a glutamic acid changes the structure of haemoglobin which is less efficient at transporting oxygen. Normal haemoglobin exists as single units whether in relaxed or tensed form whereas sickle haemoglobin units bind together after dissociating with oxygen(harvard). This forms sickle haemoglobin polymers and prevents haemoglobin from undergoing ligand induced conformational changes and cooperativity regulation is no longer in

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