Hemoglobinopathies are important inherited disorders with considerable high prevalence in Asia.
Hemoglobin Q-India is a
hemoglobinopathy that was first identified in India.
Hb Q-India is caused by the mutation GAC --> CAC at
codon 64 of the
alpha-1 globin gene. The correlation between this
hemoglobinopathy and
thalassemia was reported. Although primary structure of disorder
Hb Q-India is well documented, the secondary and tertiary structures, which can help explain the pathogenesis of the
Hb Q-India disorder is not known. In this study, amino acid sequence of human
alpha globin was searched using ExPASY and used for further mutation to
Hb Q-India disorder. The derived sequences,
alpha globin chains in both normal and
Hb Q-India disorder, were used for further investigation for secondary and tertiary structures. Modeling of these
proteins for secondary and tertiary structures was done using the NNPREDICT server and CPHmodels 2.0 Server, respectively. In this study, the secondary and tertiary structures of human
alpha globin chains of normal and
hemoglobin Q-India disorder are calculated and presented. Based on this information, the main difference between the predicted
alpha globin secondary structures of normal and
Hb Q-India is an extra helix in the
Hb Q-India. The predicted tertiary structure also supports this finding. The results from this study can be good data for further study on
Hb Q-India disorder, which can bring to the further understanding on this
hemoglobinopathy.