Haemoglobin Flashcards

1
Q

Why does sickling occur in deoxy form and not oxy?

A

in oxy form, rearrangement of subunits makes EF pocket inaccessible to val6.

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2
Q

What residue is mutated in sickle cell anaemia?

A

Glu6 in beta chains mutated to Valine

Hydrophobic valine can fit into pocket at EF corner of beta chain in another Hb molecule.

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3
Q

What is the hill coefficient?

A

Steepness at point at which protein half saturated with ligand.

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4
Q

Which residues are conserved and important for function in alpha and beta chains?

How do Beta chains differ?

A

His F8 (directly coordinates iron in haem).

His E7 (stabilises O2- bound form and destabilises CO bound form).

D chain is slightly longer!

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5
Q

outline the role of haem in haemoglobin.

A

incorporated into protein during synthesis.

Non-covalently bound but hydrophobic residues in protein interior protect oxidation of Fe2+ to Fe3+.

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6
Q

What does a sigmoid all curve allow?

A

Full saturation in lungs and maximal release at capillaries.

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