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

0424754 - ÚOCHB 2014 RIV NL eng J - Journal Article
Emmer, J. - Vavrinská, A. - Sychrovský, Vladimír - Benda, Ladislav - Kříž, Z. - Koča, J. - Boelens, R. - Sklenář, V. - Trantírek, L.
Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic N-15 chemical shielding anisotropy tensors.
Journal of Biomolecular NMR. Roč. 55, č. 1 (2013), s. 59-70. ISSN 0925-2738. E-ISSN 1573-5001
R&D Projects: GA ČR GAP205/10/0228
Grant - others:CEITEC(XE) CZ.1.05/1.1.00/02.0068
Institutional support: RVO:61388963
Keywords : CSA * phosphorylation * amidic nitrogen * serine * threonine * tyrosine * protein * NMR
Subject RIV: CE - Biochemistry
Impact factor: 3.305, year: 2013

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.
Permanent Link: http://hdl.handle.net/11104/0230810