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![[Figure 9]](tc5011fig9mag.jpg)
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Figure 9
Spectra of standard proteins in aqueous solution (H2O baseline subtracted, triplicate scans averaged). (a) Spectra from α-helix-rich proteins myoglobin, BSA and β-strand-rich protein concanavalin A, in mean residue ellipticity units. (b) SDS-PAGE analysis of proteins for CD measurements. Concanavalin A (1 µg in lane 1), myoglobin (1 µg in lane 2) and BSA (1.5 µg in lane 3) were separated using a 12.5% SDS-gel. Proteins in the resultant gel were stained with Coomassie blue. (c) CD spectra; linear dependence on concentration of these three standard proteins. Each magnitude of the CD signal for various electronic transitions exhibits a linear relation with protein concentration. Filled down triangles: data points under mis-recorded condition caused by excessive concentration of protein. Symbols of electronic transition: π–π* perpendicular (ππ*⊥); π–π* parallel (ππ*∥); π–π* (ππ*); n–π* (nπ*). All spectra were recorded with varied combination of protein concentration in a CaF2 cell (path length 7 µm), time constant 1 s and wavelength increment 0.6 nm at 298 K. |
![[Figure 9]](tc5011fig9.jpg)
 | JOURNAL OF SYNCHROTRON RADIATION |
ISSN: 1600-5775
