Reference : A nondetergent sulfobetaine improves protein unfolding reversibility in microcalorime...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/16595
A nondetergent sulfobetaine improves protein unfolding reversibility in microcalorimetric studies
English
D'Amico, Salvino [Université de Liège - ULg > > GIGA-Research >]
Feller, Georges mailto [Université de Liège - ULg > Département des sciences de la vie > Labo de biochimie >]
2009
Analytical Biochemistry
Academic Press
385
2
389-91
Yes (verified by ORBi)
International
0003-2697
1096-0309
Orlando
FL
[en] Betaine/*analogs & derivatives/chemistry ; Calorimetry, Differential Scanning/*methods ; Hydrogen-Ion Concentration ; Microchemistry ; *Protein Denaturation ; *Protein Folding ; Research Design
[en] 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.
http://hdl.handle.net/2268/16595
2008/12/09

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