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Thermal denaturation of some proteins and its effect on their electrospray mass spectrat

✍ Scribed by J. C. Y. Le Blanc; D. Beuchemin; K. W. M. Siu; R. Guevremont; S. S. Berman

Publisher
John Wiley and Sons
Year
1991
Tongue
English
Weight
832 KB
Volume
26
Category
Article
ISSN
1076-5174

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✦ Synopsis

Abstract

The 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 Δ__H__ 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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