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Updated: Jun 27, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
A nondetergent sulfobetaine improves protein unfolding reversibility in microcalorimetric studies
Salvino D'Amico1, Georges Feller
1Laboratory of Biochemistry, University of Liège, Institute of Chemistry B6a, Liège-Sart Tilman, Belgium.
Abstract:
A nondetergent sulfobetaine (NDSB) was found to improve unfolding reversibility of several proteins by inhibiting heat-induced aggregation. As a consequence, DeltaH(cal)/DeltaH(vH) 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 DeltaC(p) 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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