A nondetergent sulfobetaine improves protein unfolding reversibility in microcalorimetric studies

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 :

Pages :

389-91

Peer reviewed :

Peer Reviewed verified by ORBi

Commentary :

2008/12/09

Available on ORBi :

since 26 January 2010

Statistics

Number of views

77 (4 by ULiège)

Number of downloads

0 (0 by ULiège)

More statistics

Scopus citations^®

Scopus citations^®
without self-citations

OpenCitations

OpenAlex citations

Bibliography

Makhatadze G.I., and Privalov P.L. Energetics of protein structure. Adv. Protein Chem. 47 (1995) 307-425
Jelesarov I., and Bosshard H.R. Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J. Mol. Recognit. 12 (1999) 3-18
Kumar S., Tsai C.J., and Nussinov R. Maximal stabilities of reversible two-state proteins. Biochemistry 41 (2002) 5359-5374
Remmele Jr. R.L., Zhang-van Enk J., Dharmavaram V., Balaban D., Durst M., Shoshitaishvili A., and Rand H. Scan-rate-dependent melting transitions of interleukin-1 receptor (type II): Elucidation of meaningful thermodynamic and kinetic parameters of aggregation acquired from DSC simulations. J. Am. Chem. Soc. 127 (2005) 8328-8339
Collins T., D'Amico S., Georlette D., Marx J.-C., Huston A.L., and Feller G. A nondetergent sulfobetaine prevents protein aggregation in microcalorimetric studies. Anal. Biochem. 352 (2006) 299-301
Feller G., d'Amico D., and Gerday C. Thermodynamic stability of a cold-active α-amylase from the Antarctic bacterium Alteromonas haloplanktis. Biochemistry 38 (1999) 4613-4619
Vuillard L., Braun-Breton C., and Rabilloud T. Non-detergent sulphobetaines: A new class of mild solubilization agents for protein purification. Biochem. J. 305 (1995) 337-343
Sonan G.K., Receveur-Brechot V., Duez C., Aghajari N., Czjzek M., Haser R., and Gerday C. The linker region plays a key role in the adaptation to cold of the cellulase from an Antarctic bacterium. Biochem. J. 407 (2007) 293-302
Lepock J.R., Ritchie K.P., Kolios M.C., Rodahl A.M., Heinz K.A., and Kruuv J. Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation. Biochemistry 31 (1992) 12706-12712