Temperature dependence of ESR spectra of spin-labelled met-hemoglobin.
The maleimide spin-label, firmly fixed to the protein, was used to study conformation changes of various met-hemoglobin derivatives. The temperature dependence of the rotational correlation time shows a distinct conformation change in aquomet-hemoglobin at about 25 degrees C. The other met-hemoglobin derivatives studied (fluoro-, cyano-, aquomet-complexed with inositol hexaphosphate) and carbonmonoxy-hemoglobin exhibit no conformation changes in the temperature range from 0-50 degrees C.
D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D008301:Maleimides; D008706:Methemoglobin; D011485:Protein Binding; D011487:Protein Conformation; D013113:Spin Labels; D013696:Temperature; D013816:Thermodynamics
D008301:Maleimides; D013113:Spin Labels; D008706:Methemoglobin