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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| Authors: | Zakharov M N Ulloor J Bhasin S Ross J A Narula N S Bakhit M Pillai B K Kumar R Jameson D M Jasuja R |
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| Institution: | aSection of Endocrinology, Diabetes, and Nutrition, Boston University School of Medicine, Boston, MA 02118, USA;bDepartment of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawai‘i at Manoa, Honolulu, HI 96813, USA;cDepartment of Basic Sciences, Commonwealth Medical College, Scranton, PA 18510, USA |
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| 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. |
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