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

J 2013

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

EMMER, Jiří; Andrea VAVRINSKÁ; Vladimír SYCHROVSKÝ; Ladislav BENDA; Zdeněk KŘÍŽ et. al.

Základní údaje

Originální název

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

Autoři

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

Vydání

Journal of biomolecular NMR, Dordrecht, Springer, 2013, 0925-2738

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.305

Kód RIV

RIV/00216224:14740/13:00068469

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1007/s10858-012-9686-6

UT WoS

000314050700006

Klíčová slova anglicky

CSA; Phosphorylation; Amidic nitrogen; Serine; Threonine; Tyrosine; Protein; NMR

Štítky

ok, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 6. 4. 2014 06:04, Olga Křížová

Anotace

V originále

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.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

Citovat

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://doi.org/10.1007/s10858-012-9686-6.

@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 = {https://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://doi.org/10.1007/s10858-012-9686-6.

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