| Literature DB >> 19059190 |
Salvino D'Amico1, Georges Feller.
Abstract
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.Entities:
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Year: 2008 PMID： 19059190 DOI： 10.1016/j.ab.2008.11.016
Source DB: PubMed Journal: Anal Biochem ISSN： 0003-2697 Impact factor: 3.365