jp4028113_si_001.pdf (1.03 MB)
Dodine as a Protein Denaturant: The Best of Two Worlds?
journal contribution
posted on 2013-10-24, 00:00 authored by Hannah Gelman, Tatyana Perlova, Martin GruebeleTraditional denaturants such as urea
and guanidinium ion unfold
proteins in a cooperative “all-or-none” fashion. However,
their high working concentration in combination with their strong
absorption in the far ultraviolet region make it impossible to measure
high quality circular dichroism or infrared spectra, which are commonly
used to detect changes in protein secondary structure. On the other
hand, detergents such as dodecyl sulfate destabilize native protein
conformation at low millimolar concentrations and are UV transparent,
but they denature proteins more gradually than guanidinium or urea.
In this work, we studied the denaturation properties of the fungicide
dodecylguanidinium acetate (dodine), which combines both denaturants
into one. We show that dodine unfolds some small proteins at millimolar
concentrations, facilitates temperature denaturation, and is transparent
enough at its working concentration, unlike guanidinium, to measure
full range circular dichroism spectra. Our results also suggest that
dodine allows fine-tuning of the protein’s unfolded state,
unlike traditional “all-or-none” denaturants.