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Tertiary structural analysis of the elongated part of an abnormal hemoglobin, hemoglobin Pakse

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Authors: Viroj Wiwanitkit

Published Date January 2006 Volume 2006:1(1) Pages 105 - 107
DOI: http://dx.doi.org/10.2147/IJN.S

Viroj Wiwanitkit

Department of Laboratory Medicine, Faculty of Medicine, Chulalongkorn University, Bangkok, Thailand

Abstract: Hemoglobin variants in which a frameshift results in chain elongation are unusual. Hemoglobin Pakse (Hb Pakse) is an unstable hemoglobin with abnormal elongation, first described in Indochina. An alpha2-globin gene termination codon mutation, TAA → TAT or Term → Tyr, has been described in the pathogenesis of Hb Pakse. This abnormality causes a frameshift that elongates the alpha chain amino acids. Computer-based protein structure modeling was used in a bioinformatics analysis of the tertiary structure of these elongated amino acid sequences. The elongated part of Hb Pakse showed additional helices, which may cause the main alteration in Hb Pakse. Abnormalities in the fold structure of globin in Hb Pakse were identified, and helices additional to the normal alpha globin chains were shown in the elongated part of Hb Pakse.

Keywords: hemoglobin Pakse, alpha globin, protein structure








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