Article (Scientific journals)
A nondetergent sulfobetaine improves protein unfolding reversibility in microcalorimetric studies
D'Amico, Salvino; Feller, Georges
2009In Analytical Biochemistry, 385 (2), p. 389-91
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Keywords :
Betaine/*analogs & derivatives/chemistry; Calorimetry, Differential Scanning/*methods; Hydrogen-Ion Concentration; Microchemistry; *Protein Denaturation; *Protein Folding; Research Design
Abstract :
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
D'Amico, Salvino ;  Université de Liège - ULiège > GIGA-Research
Feller, Georges ;  Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie
Language :
English
Title :
A nondetergent sulfobetaine improves protein unfolding reversibility in microcalorimetric studies
Publication date :
2009
Journal title :
Analytical Biochemistry
ISSN :
0003-2697
eISSN :
1096-0309
Publisher :
Academic Press, Orlando, United States - Florida
Volume :
385
Issue :
2
Pages :
389-91
Peer reviewed :
Peer Reviewed verified by ORBi
Commentary :
2008/12/09
Available on ORBi :
since 26 January 2010

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