Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded -- Data Supplement - Supporting Information -- Proceedings of the National Academy of Sciences

Supporting information for Denning et al. (2003) Proc. Natl. Acad. Sci. USA, 10.1073/pnas.0437902100

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Fig. 5.
(A) FTIR spectra of the amide I region of purified Nups at pH 6.8 (dashed line) were obtained as described (10). The curve fit spectrum is presented by the solid lines. Major β-structure peaks are in the 1,620–1,640 cm^–1 region, whereas major disordered and α-helix structure peaks are in the 1,650–1,660 cm^–1 region. Only in the case of Nup85p, the deconvolved peak at 1,656 cm^–1 was attributed to α-helix structures (Table 3) based on the narrowness of the absorbance peak and the CD spectrum of Nup85p (Fig. 3). FG Nups were mostly devoid of α-helix structure (Fig. 3).