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![[Figure 2]](ys5021fig2mag.jpg)
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Figure 2
CD spectra of RseA in the absence or presence of bound RseB. (a) Calculated CD spectrum of RseA169–186 (red) generated by subtracting the spectrum of His–Trx (green) from that of His–Trx–RseA169–186 (blue). The CD spectrum indicates that the RseB binding motif of RseA is random coiled in solution. (b) CD spectrum of synthesized RseA169–186 peptide. It shows a similar pattern to the calculated CD spectrum of RseA169–186. (c) CD spectra of the periplasmic domain of RseA (RseA121–216) in free (red) and bound (light blue) states, which is obtained by subtracting the spectrum of free RseB from that of RseA121–216/RseB. (d) Calculated CD spectrum of RseA169–186 (red) generated by subtracting the spectrum of free RseB (blue) from that of the RseA169–186/RseB complex (green). This spectrum shows the presence of helical components, thereby suggesting that the RseB binding motif of RseA might have acquired some helical properties upon RseB binding. |
![[Figure 2]](ys5021fig2.jpg)
 | JOURNAL OF SYNCHROTRON RADIATION |
ISSN: 1600-5775
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