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

Copyright information: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"Nucleic Acids Research 2007;35(9):2861-2874.Published online 11 Apr 2007PMCID:PMC18888...

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Hauptverfasser: Nitharwal, Ram Gopal, Subhankar Paul, Dar, Ashraf, Nirupam Roy Choudhury, Soni, Rajesh K, Dhaneswar Prusty, Sukrat Sinha, Kashav, Tara, Gauranga Mukhopadhyay, Chaudhuri, Tapan Kumar, Samudrala Gourinath, Dhar, Suman Kumar
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Zusammenfassung:Copyright information: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"Nucleic Acids Research 2007;35(9):2861-2874.Published online 11 Apr 2007PMCID:PMC1888833.© 2007 The Author(s) 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.
DOI:10.6084/m9.figshare.57053