() Far-UV circular dichroism spectra of wild-type and different mutant variants of the helicase

<p><b>Copyright information:</b></p><p>Taken from "The domain structure of DnaB helicase: the N-terminal domain can be dispensable for helicase activity whereas the extreme C-terminal region is essential for its function"</p><p></p><p>Nucleic Acids Research 2007;35(9):2861-2874.</p><p>Published online 11 Apr 2007</p><p>PMCID:PMC1888833.</p><p>© 2007 The Author(s)</p> CD spectra were measured for each protein in a 2 mm path length quartz cell and data were collected at 1.0 nm wavelength resolution. The arrowheads indicate the CD spectra of the respective protein. () Intrinsic fluorescence spectra of wild-type and different deletion mutants. The fluorescence emission spectra of wild-type and different mutant forms of HpDnaB (as indicated) were recorded from 300 to 400 nm at 25°C. The excitation wavelength was 278 nm and data were collected at 0.5 nm wavelengths resolution. The arrowheads indicate the CD spectra of the respective protein