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.

Basic information

Original name

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

Authors

EMMER, Jiří (203 Czech Republic), Andrea VAVRINSKÁ (528 Netherlands), Vladimír SYCHROVSKÝ (203 Czech Republic), Ladislav BENDA (203 Czech Republic), Zdeněk KŘÍŽ (203 Czech Republic, belonging to the institution), Jaroslav KOČA (203 Czech Republic, belonging to the institution), Rolf BOELENS (528 Netherlands), Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution) and Lukáš TRANTÍREK (203 Czech Republic, guarantor, belonging to the institution)

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 3.305

RIV identification code

RIV/00216224:14740/13:00068469

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000314050700006

Keywords in English

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

Abstract

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.

Links

ED1.1.00/02.0068, research and development project

Name: CEITEC - central european institute of technology

Citovat

EMMER, Jiří, Andrea VAVRINSKÁ, Vladimír SYCHROVSKÝ, Ladislav BENDA, Zdeněk KŘÍŽ, Jaroslav KOČA, Rolf BOELENS, Vladimír SKLENÁŘ and 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, vol. 55, No 1, p. 59-70. ISSN 0925-2738. Available from: https://dx.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 = {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 and 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, vol.~55, No~1, p.~59-70. ISSN~0925-2738. Available from: https://dx.doi.org/10.1007/s10858-012-9686-6.

Detailed Information on Publication Record