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Comparative analysis of protein structure of common Hb Q variants.

CONTEXT
Hemoglobin (Hb) Q variant is a group of hemoglobinopathies prevalent in south, south-east and western Asia. The primary structure of all of these molecules is well known. However, very little is known about the secondary and tertiary structures of these molecules. Therefore, a study of their secondary and tertiary structures is needed.


AIM
The study was aimed at investigating the secondary and tertiary structures of common Hb Q variants using bioinformatics tool.


SETTINGS AND DESIGN
The secondary and tertiary structures of common Hb Q variants were evaluated using NNPREDICT server and CPHmodels 2.0 server, respectively.


MATERIALS AND METHODS
Amino acid sequence of alpha globin chain was searched using ExPASY and was used for further mutation to Hb Q variants. The derived sequences were further analyzed using NNPREDICT server and CPHmodels 2.0 server to calculate their secondary and tertiary structures, respectively. These were then compared and any differences noted.


RESULTS
It was observed that there is no difference between the predicted secondary structures of normal alpha globin and Hb Q-India. Hb Q-Iran carries an extra helix while Hb Q-Thailand carries two extra helices. The results of tertiary structure prediction also support these findings.


CONCLUSIONS
Differences in secondary and tertiary structure of various Hb Q variants have been observed in the present study. The study provides valuable data for better understanding of these uncommon hemoglobinopathies.