Nuclear magnetic resonance assignments and secondary structure of bovine S100β protein

Peter M. Kilby, Linda J. Van Eldik, Gordon C.K. Roberts

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


S100β is a neurite extension factor and has been implicated in Alzheimer's disease and Down's syndrome. It belongs to a group of low molecular weight calcium-binding proteins containing the helix-loop-helix calcium binding motif. The structure of only one S100 protein, calbindin D9k, which has the lowest sequence similarity to the other members of the S100 group has been determined. We report the NMR assignments and secondary structure of calcium-free S100β. The secondary structure is similar to that of calbindin D9k, determined using NMR, except that there is clear evidence for an additional well ordered 5-residue α-helix in S100β.

Original languageEnglish
Pages (from-to)90-96
Number of pages7
JournalFEBS Letters
Issue number1-2
StatePublished - Apr 17 1995

Bibliographical note

Funding Information:
Acknowledgements: This work was supported by a Wellcome Trust Research Fellowship to P.M.K. and by National Institutes of Health Grant AG10208 to L.V.E.


  • Calcium-binding protein
  • Nuclear magnetic resonance
  • S-100
  • S100
  • Secondary structure

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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