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Anal Biochem. 2011 Sep 1;416(1):126-8. doi: 10.1016/j.ab.2011.04.022. Epub 2011 Apr 20.

Guanidinium chloride-induced spectral perturbations of 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid confound interpretation of data on molten globule states.

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1
Section of Endocrinology, Diabetes, and Nutrition, Boston University School of Medicine, Boston, MA 02118, USA.

Abstract

We describe limitations in the use of 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid (bis-ANS) to examine unfolding intermediates associated with guanidinium chloride (GuHCl)-induced protein denaturation. Several studies have used alterations in fluorescence emission of bis-ANS to quantify the population of "molten globule" states. Our findings indicate that the observed changes in bis-ANS spectroscopic properties could originate from the interactions of bis-ANS and GuHCl and the aggregation of the dye at higher GuHCl concentrations. We posit that in the absence of additional complementary structural or spectroscopic measurements, the use of bis-ANS emission alone to monitor protein conformations can be misleading.

PMID:
21569754
DOI:
10.1016/j.ab.2011.04.022
[Indexed for MEDLINE]

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