Abstract
Glycation and glutathionylation are important posttranslational modifications (PTMs) of human haemoglobin that act as biomarkers of diabetes mellitus and oxidative stress. These PTMs perturb the function of normal haemoglobin. However, the structure–function correlation of these PTMs of genetically modified haemoglobin remained unexplored. Using hydrogen/ deuterium exchange mass spectrometry, we studied the conformational dynamics of glycated and glutathionylated forms of two haemoglobin variants, HbE and HbD Punjab. Like glycated and glutathionylated normal haemoglobin, these PTMs of HbE were expected to have increased oxygen affinity. However, for HbD Punjab, glycation was predicted to have decreased oxygen affinity whereas glutathionylation to have increased oxygen affinity.
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