The influence of Mg2+ coordination on 13C and 15N chemical shifts in CKI1RD protein domain from experiment and molecular dynamics/density functional theory calculations

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F16%3A00087872" target="_blank" >RIV/00216224:14310/16:00087872 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1002/prot.25019" target="_blank" >http://dx.doi.org/10.1002/prot.25019</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/prot.25019" target="_blank" >10.1002/prot.25019</a>

Result language
angličtina
Original language name
The influence of Mg2+ coordination on 13C and 15N chemical shifts in CKI1RD protein domain from experiment and molecular dynamics/density functional theory calculations
Original language description
Sequence dependence of 13C and 15N chemical shifts in the receiver domain of CKI1 protein from Arabidopsis thaliana, CKI1RD, and its complexed form, CKI1RD.Mg2+, was studied by means of MD/DFT calculations. MD simulations of a 20–ns production run length were performed. Nine explicitly hydrated structures of increasing complexity were explored, up to a 40-amino-acid structure. The size of the model necessary depended on the type of nucleus, the type of amino acid and its sequence neighbors, other spatially close amino acids, and the orientation of amino acid NH groups and their surface/interior position. Using models covering a 10 and a 15 A environment of Mg2+, a semi-quantitative agreement has been obtained between experiment and theory for the V67-I73 sequence. The influence of Mg2+ binding was described better by the 15 A as compared to the 10 A model. Thirteen chemical shifts were analyzed in terms of the effect of Mg2+ insertion and geometry preparation.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Project
<a href="/en/project/GAP305%2F11%2F0756" target="_blank" >GAP305/11/0756: Structural basis for the specificity of signal transduction in plants: interaction network of histidine kinase receiver domains in Arabidopsis</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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