Solvent-induced differentiation of protein backbone hydrogen bonds in calmodulin |
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Authors: | Juranić Nenad Atanasova Elena Streiff John H Macura Slobodan Prendergast Franklyn G |
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Affiliation: | Department of Biochemistry and Molecular Biology, Mayo College of Medicine, Mayo Clinic and Foundation, Rochester, MN 55905, USA. juranic.nenad@mayo.edu |
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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. |
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Keywords: | hydrogen bonding proteins calmodulin h3JNC′ couplings |
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