Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic N-15 chemical shielding anisotropy tensors
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F13%3A00068469" target="_blank" >RIV/00216224:14740/13:00068469 - isvavai.cz</a>
Alternative codes found
RIV/61388963:_____/13:00424754
Result on the web
<a href="http://link.springer.com/content/pdf/10.1007%2Fs10858-012-9686-6.pdf" target="_blank" >http://link.springer.com/content/pdf/10.1007%2Fs10858-012-9686-6.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s10858-012-9686-6" target="_blank" >10.1007/s10858-012-9686-6</a>
Alternative languages
Result language
angličtina
Original language name
Influence of the O-phosphorylation of serine, threonine and tyrosine in proteins on the amidic N-15 chemical shielding anisotropy tensors
Original language 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.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of biomolecular NMR
ISSN
0925-2738
e-ISSN
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Volume of the periodical
55
Issue of the periodical within the volume
1
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
12
Pages from-to
59-70
UT code for WoS article
000314050700006
EID of the result in the Scopus database
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