Publication details
Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic N-15 chemical shielding anisotropy tensors
| Authors | |
|---|---|
| Year of publication | 2013 |
| Type | Article in Periodical |
| Magazine / Source | Journal of biomolecular NMR |
| MU Faculty or unit | |
| Citation | |
| Web | http://link.springer.com/content/pdf/10.1007%2Fs10858-012-9686-6.pdf |
| Doi | http://dx.doi.org/10.1007/s10858-012-9686-6 |
| Field | Biochemistry |
| Keywords | CSA; Phosphorylation; Amidic nitrogen; Serine; Threonine; Tyrosine; Protein; NMR |
| Description | 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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