Journal of Biomolecular NMR

, Volume 56, Issue 4, pp 313–329 | Cite as

13C structuring shifts for the analysis of model β-hairpins and β-sheets in proteins: diagnostic shifts appear only at the cross-strand H-bonded residues

  • Irene Shu
  • Michele Scian
  • James M. Stewart
  • Brandon L. Kier
  • Niels H. Andersen


The present studies have shown that 13C=O, 13Cα and 13Cβ of H-bonded strand residues in β-hairpins provide additional probes for quantitating the extent of folding in β-hairpins and other β-sheet models. Large differences in the structuring shifts (CSDs) of these 13C sites in H-bonded versus non-H-bonded sites are observed: the differences between H-bonded and non-H-bonded sites are greater than 1.2 ppm for all three 13C probes. This prompts us to suggest that efforts to determine the extent of hairpin folding from 13C shifts should be based exclusively on the observation at the cross-strand H-bonded sites. Furthermore, the statistics suggest the 13C′ and 13CβCSDs will provide the best differentiation with 100 %-folded CSD values approaching −2.6 and +3 ppm, respectively, for the H-bonded sites. These conclusions can be extended to edge-strands of protein β-sheets. Our survey of reported 13C shifts in β-proteins indicates that some of the currently employed random coil values need to be adjusted, particularly for ionization-induced effects.


β-hairpin β-sheet 13C chemical shift deviations Folding probes 13C statistical coil shifts 



This work was supported by the National Science Foundation (grants CHE-0650318 and -1152218).

Supplementary material

10858_2013_9749_MOESM1_ESM.pdf (648 kb)
Supplementary material 1 (PDF 648 kb)


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Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  • Irene Shu
    • 1
  • Michele Scian
    • 1
  • James M. Stewart
    • 1
  • Brandon L. Kier
    • 1
  • Niels H. Andersen
    • 1
  1. 1.Department of ChemistryUniversity of WashingtonSeattleUSA

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