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 language | English (US) |
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Pages (from-to) | 1329-1337 |
Number of pages | 9 |
Journal | Protein Science |
Volume | 16 |
Issue number | 7 |
DOIs | |
State | Published - Jul 2007 |
Keywords
- Calmodulin
- Hydrogen bonding
- J couplings
- Proteins
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology