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Srinivasu, Bindu Y.
- Functional Prediction from Conformational Dynamics of Glycated and Glutathionylated HbE and HbD Punjab
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Authors
Sreekala Narayanan
1,
Boby Mathew
1,
Bindu Y. Srinivasu
1,
Monita Muralidharan
1,
Vijay Bhat
2,
Amit Kumar Mandal
1
Affiliations
1 Clinical Proteomics Unit, Division of Molecular Medicine, St John’s Research Institute, St John’s National Academy of Health Sciences, Bengaluru 560 034, IN
2 Manipal Hospital, Old Airport Road, Bengaluru 560 017, IN
1 Clinical Proteomics Unit, Division of Molecular Medicine, St John’s Research Institute, St John’s National Academy of Health Sciences, Bengaluru 560 034, IN
2 Manipal Hospital, Old Airport Road, Bengaluru 560 017, IN
Source
Current Science, Vol 118, No 5 (2020), Pagination: 722-727Abstract
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.Keywords
Glutathionylation, HbE, HbD Punjab, Glycation, Post-Translational Modifications, Structure–Function Correlation.Full Text
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