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. Author manuscript; available in PMC: 2008 Aug 28.
Published in final edited form as: Biochemistry. 2007 May 19;46(23):6774–6783. doi: 10.1021/bi700391b

Figure 2.

Figure 2

Effect of Mn-induced PRE on the resonance intensities. (A) Amino acid sequence of human FXYD1 with helical regions underlined. Residue numbering begins at 1 after the signal sequence (NCBI protein accession: NP_068702). (B) Protein secondary structure. (C) 1H/15N heteronuclear NOEs. (D) Normalized 1H/15N HSQC peak intensities obtained without (I−Mn, black bars) or with (I+Mn, gray bars) 1.6 mM MnCl2. Positions that are left blank correspond to prolines (P3, P8, P53) or overlapped resonances (E5, A24). (E) Residual normalized peak intensity (I−Mn/I+Mn). The horizontal square brackets mark residues in H3 and H4 with similar protection from aqueous Mn.