Melting of Hemoglobin in Native Solutions as measured by IMS-MS.

ABSTRACT: Thermally induced structural transitions of the quaternary structure of the hemoglobin tetramer (human) in aqueous solution (150 mM ammonium acetate) were investigated using a variable temperature electrospray ionization (vt-ESI) technique in combination with ion mobility spectrometry (IMS) and mass spectrometry (MS) measurements. At low solution temperatures (28 to ∼40 °C), a heterotetrameric (α₂β₂) complex is the most abundant species that is observed. When the solution temperature is increased, this assembly dissociates into heterodimers (holo αβ forms) before ultimately forming insoluble aggregates at higher temperatures (>60 °C). In addition to the holo αβ forms, a small population of αβ dimers containing only a single heme ligand and having a dioxidation modific

SUBMITTER: Woodall DW 

PROVIDER: S-EPMC7480357 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature