The Arg114Pro amino acid substitution would produce a change from a hydrophilic positively charged, polar amino acid on the amino-terminal domain (residues 1-164) to a hydrophobic nonpolar amino acid
. This might then affect receptor binding.
The colour intensity of MRP from basic amino acids was reportedly greater than that of acidic amino acids, while nonpolar amino acids
were of intermediate colour intensity.
The replacement of P92S and A277T were conversion of non-polar to polar amino acids whereas the change of T156A T191A and T239M were from polar to nonpolar amino acids
. The presence of X at position 193 in the reference sequence of P.
Such conservative changes could represent replacements of both amino acids with identical chemical proprieties (for example, the substitutions evaluated in this study occurred among hydrophobic, nonpolar amino acids
In sickle cell anemia, these glutamic acids are replaced by valines, large nonpolar amino acids
. The sickle cell hemoglobins aggregate into chains thousands of molecules long, as valines on adjacent hemoglobin molecules are attracted by hydrophobic interactions.