A nondetergent sulfobetaine improves protein unfolding reversibility in microcalorimetric studies |
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| Authors: | Salvino D’Amico |
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| Institution: | Laboratory of Biochemistry, University of Liège, Institute of Chemistry B6a, B-4000 Liège-Sart Tilman, Belgium |
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| Abstract: | A nondetergent sulfobetaine (NDSB) was found to improve unfolding reversibility of several proteins by inhibiting heat-induced aggregation. As a consequence, ΔHcal/ΔHvH ratios were also improved to values close to 1 for a two-state unfolding. NDSB is effective in a wide range of pH values and especially at acidic pH generally used to calculate ΔCp values by the Kirchhoff relation. The sulfobetaine also allows recording protein refolding by protecting the heat-induced unfolded state against aggregation. |
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