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Solvent-induced differentiation of protein backbone hydrogen bonds in calmodulin

Nenad Jurani¹, Elena Atanasova², John H. Streiff³, Slobodan Macura¹, and Franklyn G. Prendergast^1,2

¹ Department of Biochemistry and Molecular Biology, Mayo College of Medicine, Mayo Clinic and Foundation, Rochester, Minnesota 55905, USA
² Department of Molecular Pharmacology and Experimental Therapeutics, Mayo College of Medicine, Mayo Clinic and Foundation, Rochester, Minnesota 55905, USA
³ Department of Anesthesiology, Mayo College of Medicine, Mayo Clinic and Foundation, Rochester, Minnesota 55905, USA

(RECEIVED November 28, 2006; FINAL REVISION February 18, 2007; ACCEPTED February 23, 2007)

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 ^h3 J _NC' couplings. The paucity of the ^h3 J _NC' 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 ^h3 J _NC' couplings measured in solution. H-bonds that have ^h3 J _NC' 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.

Keywords: hydrogen bonding; proteins; calmodulin; ^h3 J _NC' couplings

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