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. 2008 Mar 7;94(12):4847–4866. doi: 10.1529/biophysj.107.125823

FIGURE 2.

FIGURE 2

Chemical shift difference plots (A) HN, (B) N, (C) Hα, (D) Cβ, (E) Cα, for rmMBP in 30% TFE-d2 at 300 K. The random coil values for HN, N, Hα, and Cα have been adjusted for sequence dependence as previously described for the Golli-MBP isoform rmBG21 (64). The dashed lines in all the panels indicate the minimum threshold values for the formation of secondary structure elements. Generally, a consecutive stretch of four residues above the threshold value, or three residues below the threshold value, is considered to be an α-helical or β-strand element, respectively.