| EMMER, Jiří, Andrea VAVRINSKÁ, Vladimír SYCHROVSKÝ, Ladislav BENDA, Zdeněk KŘÍŽ, Jaroslav KOČA, Rolf BOELENS, Vladimír SKLENÁŘ a Lukáš TRANTÍREK. 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. Dordrecht: Springer, 2013, roč. 55, č. 1, s. 59-70. ISSN 0925-2738. Dostupné z: https://dx.doi.org/10.1007/s10858-012-9686-6. |
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@article{1110023,
author = {Emmer, Jiří and Vavrinská, Andrea and Sychrovský, Vladimír and Benda, Ladislav and Kříž, Zdeněk and Koča, Jaroslav and Boelens, Rolf and Sklenář, Vladimír and Trantírek, Lukáš},
article_location = {Dordrecht},
article_number = {1},
doi = {http://dx.doi.org/10.1007/s10858-012-9686-6},
keywords = {CSA; Phosphorylation; Amidic nitrogen; Serine; Threonine; Tyrosine; Protein; NMR},
language = {eng},
issn = {0925-2738},
journal = {Journal of biomolecular NMR},
title = {Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic N-15 chemical shielding anisotropy tensors},
url = {http://link.springer.com/content/pdf/10.1007%2Fs10858-012-9686-6.pdf},
volume = {55},
year = {2013}
}
TY - JOUR
ID - 1110023
AU - Emmer, Jiří - Vavrinská, Andrea - Sychrovský, Vladimír - Benda, Ladislav - Kříž, Zdeněk - Koča, Jaroslav - Boelens, Rolf - Sklenář, Vladimír - Trantírek, Lukáš
PY - 2013
TI - Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic N-15 chemical shielding anisotropy tensors
JF - Journal of biomolecular NMR
VL - 55
IS - 1
SP - 59-70
EP - 59-70
PB - Springer
SN - 09252738
KW - CSA
KW - Phosphorylation
KW - Amidic nitrogen
KW - Serine
KW - Threonine
KW - Tyrosine
KW - Protein
KW - NMR
UR - http://link.springer.com/content/pdf/10.1007%2Fs10858-012-9686-6.pdf
L2 - http://link.springer.com/content/pdf/10.1007%2Fs10858-012-9686-6.pdf
N2 - 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.
ER -
EMMER, Jiří, Andrea VAVRINSKÁ, Vladimír SYCHROVSKÝ, Ladislav BENDA, Zdeněk KŘÍŽ, Jaroslav KOČA, Rolf BOELENS, Vladimír SKLENÁŘ a Lukáš TRANTÍREK. Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic N-15 chemical shielding anisotropy tensors. \textit{Journal of biomolecular NMR}. Dordrecht: Springer, 2013, roč.~55, č.~1, s.~59-70. ISSN~0925-2738. Dostupné z: https://dx.doi.org/10.1007/s10858-012-9686-6.
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