Solvent-induced differentiation of protein backbone hydrogen bonds in calmodulin

Nenad Juranić, Elena Atanasova, John H. Streiff, Slobodan Macura, Franklyn G. Prendergast

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

In apo and holoCaM, almost half of the hydrogen bonds (H-bonds) at the protein backbone expected from the corresponding NMR or X-ray structures were not detected by h3JNC′ couplings. The paucity of the h3JNC′ couplings was considered in terms of dynamic features of these structures. We examined a set of seven proteins and found that protein-backbone H-bonds form two groups according to the h3JNC′ couplings measured in solution. H-bonds that have h3JNC′ couplings above the threshold of 0.2 Hz show distance/angle correlation among the H-bond geometrical parameters, and appear to be supported by the backbone dynamics in solution. The other H-bonds have no such correlation; they populate the water-exposed and flexible regions of proteins, including many of the CaM helices. The observed differentiation in a dynamical behavior of backbone H-bonds in apo and holoCaM appears to be related to protein functions. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)1329-1337
Number of pages9
JournalProtein Science
Volume16
Issue number7
DOIs
StatePublished - Jul 1 2007

Keywords

  • Calmodulin
  • Hydrogen bonding
  • J couplings
  • Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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    Juranić, N., Atanasova, E., Streiff, J. H., Macura, S., & Prendergast, F. G. (2007). Solvent-induced differentiation of protein backbone hydrogen bonds in calmodulin. Protein Science, 16(7), 1329-1337. https://doi.org/10.1110/ps.062689807