Comparative analysis of protein structure of common Hb Q variants

• Main Author: Yadav Amit
• Format: Article
• Language: English
• Published: Wolters Kluwer Medknow Publications 2010-10-01
• Series: Indian Journal of Pathology and Microbiology
• Subjects: Bioinformatics; Hb Q; protein structure
• Online Access: http://www.ijpmonline.org/article.asp?issn=0377-4929;year=2010;volume=53;issue=4;spage=696;epage=698;aulast=Yadav

<b>Context:</b> 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. <b>Aim:</b> The study was aimed at investigating the secondary and tertiary structures of common Hb Q variants using bioinformatics tool. <b>Settings and Design:</b> The secondary and tertiary structures of common Hb Q variants were evaluated using NNPREDICT server and CPHmodels 2.0 server, respectively. <b>Materials and Methods:</b> 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. <b>Results:</b> 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. <b>Conclusions:</b> 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.