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. 2015 May 1;26(9):1764–1781. doi: 10.1091/mbc.E14-10-1475

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© 2015 Ghosh, de Campos, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 3: — NMR analyses of AtSfh1 nodulin peptide binding to PtdIns(4,5)P₂. The ¹H NMR spectra of three AtSfh1 nodulin peptide variants (peptide sequences given at bottom; Lys → Ala highlighted in red) are stacked and color coded according to di-C₄-PtdIns(4,5)P₂:peptide molar ratio. Three ¹H spectral regions are shown: amide (A), aromatic (B), and upfield methyl (0.75–1.05 ppm; C). Significant chemical shift changes resulting from di-C₄-PtdIns(4,5)P₂ binding to nodulin peptide are marked (vertical lines). Peaks centered at 0.91 ppm correspond to methyl protons of di-C₄-PtdIns(4,5)P₂ acyl chains. The Leu Hδ peak of di-C₄-PtdIns(4,5)P₂-bound peptides is marked by an asterisk.