Directly observed hydrogen bonds at calcium-binding-sites of calmodulin in solution relate to affinity of the calcium-binding

Nenad Juranić, Elena Atanasova, Slobodan Macura, Franklyn G. Prendergast

Research output: Contribution to journalArticle

1 Scopus citations


Molecular tuning to calcium-binding in the EF-hand motif of holo-calmodulin was studied in solution by NMR h3JNC′ H-bond couplings. In the N-terminus lobe of holo-calmodulin, the glutamate crucial for Ca2+ coordination has network of H-bonds weaker than inferred from the X-ray crystal structure. This glutamate at position 12 appears shifted away from the Ca2+ preferred coordination, which can explain the lower affinity of the calcium-binding to the N-terminus with respect to C-terminus EF hands.

Original languageEnglish (US)
Pages (from-to)1415-1418
Number of pages4
JournalJournal of Inorganic Biochemistry
Issue number10
StatePublished - Oct 1 2009



  • Calcium-binding
  • Calmodulin
  • Hydrogen bonds
  • NMR J couplings
  • Protein structure

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

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