Molecular insights of inhibition in sickle hemoglobin polymerization upon glutathionylation: hydrogen/deuterium exchange mass spectrometry and molecular dynamics simulation-based approach
Global conformational changes in IgG-Fc upon mutation of the FcRn-binding site are not associated with altered antibody-dependent effector functions
Illustration of the role of glutathione in the inhibition of sickle hemoglobin polymerization: Two hemoglobin tetramers are shown in the surface representation and helical cartoon, wherein α and β globin chains are coloured magenta and cyan, respectively. The proximity of covalently bound glutathione to βCys93, represented as stick model, to the residues of the groove region is shown in yellow in the inset. βVal6 of the adjacent tetramer, the key residue in the polymerisation, is shown in spacefill model; For details, see pages 2153–2166. Image kindly provided by Amit Kumar Mandal.