The structure of a protein defines its functions and biophysical properties. Gel electrophoresis and liquid chromatography experiments establish that HbE has a different surface property compared to HbA. Therefore, we do expect structural variations in HbE. Changes in the structure may reflect on the glutathionylation pattern of HbE. In this proposed project, we intend to analyse the structural differences in HbA and HbE and assess the functional differences in terms of its glutathionylation property.
Glutathionyl haemoglobin has been found to be a biomarker for oxidative stress in several medical conditions. Information about the phenomena of glutathionylation of Hb variants is limited. Information regarding the changes caused to the rate and extent of glutathionylation due to the presence of the mutation in Hb is not sufficient. HbE being one of the most commonly occurring haemoglobin variants in our country, investigating these issues can give a better insight about understanding the glutathionylation of Hb variants which serves as a marker for oxidative stress.