Guanidinium chloride-induced spectral perturbations of 4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acid confound interpretation of data on molten globule states
| Autor: | Jagadish Ulloor, Shalender Bhasin, Mikhail N. Zakharov, M. Bakhit, David M. Jameson, Raj Kumar, Justin A. Ross, Biju K. Pillai, Ravi Jasuja, Navjot S. Narula |
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| Rok vydání: | 2011 |
| Předmět: |
Guanidinium chloride
Protein Denaturation education.field_of_study Dose-Response Relationship Drug Protein Conformation Chemistry Population Biophysics Proteins Cell Biology Biochemistry Fluorescence Anilino Naphthalenesulfonates Molten globule Interpretation (model theory) Structure-Activity Relationship Crystallography chemistry.chemical_compound Spectrometry Fluorescence education Molecular Biology Guanidine Protein Unfolding |
| Zdroj: | Analytical Biochemistry. 416:126-128 |
| ISSN: | 0003-2697 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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