Investigating effect of E۶V mutation in sickle cell anemia on -globolin structure: Bioinformatical Approach

چکیده مقاله

Normal adult hemoglobin (HbA) is a tetramer protein which made up from two and two subunits ( ). Each subunit owns an O2-carrying heme group. There is also the allele which appear in HbS that differ in a nucleotide from HbA, however, this difference results in Glu6Val amino acid substitution. This change increases the hydrophobicity of molecule that cause to hydrophobic interaction. By using different softwares, we have investigated here the effect of this mutation on the structure of -globolin from some different points of view such as phi, psi, and omega angels, and 3D structure. We have also shown that this mutation does not change the secondary structure of protein, however, it alternates the angels and 3D structure. Interestingly, these alternations not only belong to this region but also it could make hydrophobic amino acids of various part of -globolin more accessible which could explain production aggregates by hydrophobic interactions in mutant types.