Abstract
Traditional denaturants such as urea and guanidinium hydrochloride effectively unfold a variety of proteins in an “all-or-none” fashion. However their high working concentration in combination with the strong absorption below 210 nm make it impossible to measure high quality circular dichroism spectra, which are commonly used to detect changes in protein secondary structure. Detergents on the other hand destabilize native protein conformation at the extremely low concentration of several millimolar and are UV transparent, but they do not denature proteins as effectively as guanidinium or urea. In this work we studied the denaturation properties of the dodecylguanidine acetate which can be considered as a chemical combination of detergent and guanidinium. We have shown that dodecylguanidine acetate unfolds the protein at the millimolar concentration and is transparent enough to measure full range circular dichroism spectra. Our results also suggest that dodecylguanidine acetate allows to fine-tune the degree of protein unfolding unlike traditional “all-or-none” denaturants.
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