Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic N-15 chemical shielding anisotropy tensors
| Autoři | |
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| Rok publikování | 2013 |
| Druh | Článek v odborném periodiku |
| Časopis / Zdroj | Journal of biomolecular NMR |
| Fakulta / Pracoviště MU | |
| Citace | |
| www | http://link.springer.com/content/pdf/10.1007%2Fs10858-012-9686-6.pdf |
| Doi | http://dx.doi.org/10.1007/s10858-012-9686-6 |
| Obor | Biochemie |
| Klíčová slova | CSA; Phosphorylation; Amidic nitrogen; Serine; Threonine; Tyrosine; Protein; NMR |
| Popis | Density functional theory was employed to study the influence of O-phosphorylation of serine, threonine, and tyrosine on the amidic N-15 chemical shielding anisotropy (CSA) tensor in the context of the complex chemical environments of protein structures. Our results indicate that the amidic N-15 CSA tensor has sensitive responses to the introduction of the phosphate group and the phosphorylation-promoted rearrangement of solvent molecules and hydrogen bonding networks in the vicinity of the phosphorylated site. Yet, the calculated N-15 CSA tensors in phosphorylated model peptides were in range of values experimentally observed for non-phosphorylated proteins. The extent of the phosphorylation induced changes suggests that the amidic N-15 CSA tensor in phosphorylated proteins could be reasonably well approximated with averaged CSA tensor values experimentally determined for non-phosphorylated amino acids in practical NMR applications, where chemical surrounding of the phosphorylated site is not known a priori in majority of cases. Our calculations provide estimates of relative errors to be associated with the averaged CSA tensor values in interpretations of NMR data from phosphorylated proteins. |
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