Prediction of secondary and tertiary structures of hemoglobin Constant Spring

Abstract

Hemoglobin (Hb) constant spring (CS) disorder is an important hemoglobinopathy with the highest endemicity in Southeast Asia. The role of Hb CS instability in altered red cell morphology relative to the thalassemia-like deficit of alpha globin mRNA has not been entirely resolved and needs additional structural study for clarification. Here, amino acid sequence of human alpha globin was extracted using ExPASY and used for further mutated to Hb CS disorder. The derived sequences, alpha globin chains in both normal and Hb CS disorder, were used for further investigation for secondary structures. Modeling of these proteins for secondary structure was done using the NNPREDICT server. Of interest, the secondary structure of human alpha globin chains of normal and Hb CS disorder are calculated and presented. Based on this information, the main difference between the globin chains of normal and Hb CS disorder is the elongation in the structure. Alpha globin chain of hemoglobin disorder contains more helical residues in elongated part than normal. In addition, the tertiary structure of Hb CS was also modeled using Pepstr server.