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. 2019 Jul 17;73(10):587–599. doi: 10.1007/s10858-019-00270-4

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© The Author(s) 2019

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Fig. 3 — Serine phosphorylation. a Superposition of ¹H–¹⁵N HSQC NMR spectra of random coil peptides containing serine (black contours) and phosphoserine (blue contours) as residue ‘X’. The arrow shows the characteristic ~ 0.3 ppm downfield shift of HN upon phosphorylation. b¹H–¹³C HSQC NMR spectra with shifts of Hα/Cα and Hβ/Cβ marked with arrows