Publication details

Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic N-15 chemical shielding anisotropy tensors

Authors

EMMER Jiří VAVRINSKÁ Andrea SYCHROVSKÝ Vladimír BENDA Ladislav KŘÍŽ Zdeněk KOČA Jaroslav BOELENS Rolf SKLENÁŘ Vladimír TRANTÍREK Lukáš

Year of publication 2013
Type Article in Periodical
Magazine / Source Journal of biomolecular NMR
MU Faculty or unit

Central European Institute of Technology

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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