biochem help! -- In hemoglobin, the distal and proximal histidines... 1. The problem statement, all variables and given/known data In hemoglobin, the distal and proximal histidines are critical in the function of the protein, and they are found in both α and β chains. The distal histidine corresponds to position 65 in the alignment and the proximal histidine to position 94 in the alignment. How does the sequence identity around these residues compare to the overall identity? (Consider an 11-residue block centered on the histidine). Briefly explain, in one or two sentences, why this makes sense in terms of protein structure 2. Relevant equations 3. The attempt at a solution Would the sequence identity be higher around these histidines because throughout the sequence we want conservative amino acids so the function is not changed? also the amino acids around this should be hydrophobic surrounded by hydrophillic so it get the globular shape?