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A nondetergent sulfobetaine improves protein unfolding reversibility in microcalorimetric studies

Salvino S D'Amico and Georges G Feller

Anal Biochem 385(2):3 (2009) PMID 19059190

A nondetergent sulfobetaine (NDSB) was found to improve unfolding reversibility of several proteins by inhibiting heat-induced aggregation. As a consequence, @DH"c"a"l/@DH"v"H 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 @DC"p values by the Kirchhoff relation. The sulfobetaine also allows recording protein refolding by protecting the heat-induced unfolded state against aggregation.

Copyright © 2009 Elsevier Ltd. All rights reserved.

DOI: 10.1016/j.ab.2008.11.016
Version: za2963e q8zad q8zba q8zcf q8zd8 q8zeb q8zf0 q8zg6
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