Shown attached is a helical wheel projection of one of the Alpha helices from human hemoglobin. This is an amphipathic helix with one side polar and exposed to solvent and the other side nonpolar and buried. Indicate approximately which side of the helix is likely to be in the solvent exposed and which side is likely to face the hydrophobic interior of the protein. What is the most reasonable candidate for a terminal residue in this alpha helix.
In this case it is the C-terminus but I do not understand why; please explain.
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The side of the helix likely to be exposed to the solvent side contains predominantly hydrophilic amino acid residues, and the side facing the hydrophobic interior of the protein consists of hydrophobic residues. Clue: Histidine and Aspartate ...
The solution gives a clearly-written explanation of the cause of how to reach an answer for the most reasonable candidate for a terminal residue in the alpha helix described, including a link for further reading and illustration of the occurrence.