Abstract
AbstractThe effects of beat on the electrospray mass spectra of eight globular proteins in solution were studied. These ranged from hardly noticeable to a dramatic shift in the mass spectrometric profile and a concomitant increase in ion abundance. This change is believed to be the result of thermal denaturation of the protein species in solution resulting in a transition from a more compact to a less compact conformation. We accounted for this transition by means of a recently proposed model based on aqueous solution acid/base equilibria. For cytochrome c, profiles calculated by means of this model agree well with experimental data. The ΔH of the denaturation reaction of cytochrome c in aqueous solution containing 0.2% acetic acid was calculated from experimental data to be 103.8 ± 9.2 kJ mol−1, in good agreement with previous measurements.
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