Aqueous Guanidinium-Carbonate Interactions by Molecular Dynamics and Neutron Scattering: Relevance to Ion-Protein Interactions
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F13%3A00391709" target="_blank" >RIV/61388963:_____/13:00391709 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1021/jp310719g" target="_blank" >http://dx.doi.org/10.1021/jp310719g</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/jp310719g" target="_blank" >10.1021/jp310719g</a>
Alternative languages
Result language
angličtina
Original language name
Aqueous Guanidinium-Carbonate Interactions by Molecular Dynamics and Neutron Scattering: Relevance to Ion-Protein Interactions
Original language description
Guanidinium carbonate was used in this study as a simple proxy for the biologically relevant arginine-carbonate interactions in water. Molecular dynamics (MD) simulations of guanidinium carbonate were performed with nonpolarizible water using two implementations of the ion force fields. In the first, the ions had full charges, while in the second, the ions had reduced charges in order to effectively account for electronic polarization effects of water. The results from the simulations were then comparedto data from previous neutron scattering experiments. It was found that there were significant discrepancies between the full charge force field MD simulations and the experimental results due to excessive ion pairing and clustering in the former. In contrast, reducing the ionic charges yields a more regular solution with a simulated structure, which fits well the experimental data.
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
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GBP208%2F12%2FG016" target="_blank" >GBP208/12/G016: Controlling structure and function of biomolecules at the molecular scale: theory meets experiment</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
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 Physical Chemistry B
ISSN
1520-6106
e-ISSN
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Volume of the periodical
117
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
5
Pages from-to
1844-1848
UT code for WoS article
000315181600042
EID of the result in the Scopus database
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