[jubba]

This is a nice biochem question if found and think : ) i know how to do.

Red blood cells contain the globular (water soluble) protein haemoglobin which is used to
transport oxygen about the body.
(a) Where would you expect to find the largest proportion of hydrophobic and hydrophilic amino
acids in the native structure (i.e. as found in the body) of haemoglobin? Explain briefly why
haemoglobin adopts its native 3D structure with these properties?
Sickle-cell anaemia is a disease caused by a single amino acid residue in haemoglobin being
mutated (changed), resulting in a misfolding of haemoglobin. The residue in question,
located on the surface of the haemoglobin structure, is a glutamic acid (-CH2CH2COOH
sidechain) in normal haemoglobin, whereas in mutated “S”-haemoglobin it is changed to a
valine (isopropyl sidechain).
(b) Explain using your answer to (a) how this mutation may cause haemoglobin to misfold.

[AWK]

Solve this problem independently. You can get PDB files for both haemoglobins for free and use many free programs (eg RASMOL)  to look inside of both molecules

[jubba]

i don't really have an set solution

but this is what i think

a)
Hyrophobic will be inside the haemoglobin with the hyrdophobic acids mainly will be found on the surface making the globin water soluble

b) the glutamic acid sidechain is hyrophilic so it would be on the surface whilst valine is hyrophobic causing a unnecesary fold inwards.

this is what i thought but if im wrong please correct me.

but i thought it was a nice answer

[AWK]

http://edtech.suhsd.k12.ca.us/inprogress/cvh/hhuckaby/bioweb/sicklecellgeneprofile.htm