A nondetergent sulfobetaine improves protein unfolding reversibility in microcalorimetric studies.
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.
D'Amico
Salvino
S
Laboratory of Biochemistry, University of Liège, Institute of Chemistry B6a, Liège-Sart Tilman, Belgium.
Feller
Georges
G
D001622:Betaine / Q000031:analogs & derivatives* / Q000737:chemistry; D002152:Calorimetry, Differential Scanning / Q000379:methods*; D006863:Hydrogen-Ion Concentration; D008832:Microchemistry; D011489:Protein Denaturation; D017510:Protein Folding; D012107:Research Design
D001622:Betaine; C483727:sulfobetaine