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

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Bibliography

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