Effects of end-group termination on salting-out constants for triglycine

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F13%3A00421956" target="_blank" >RIV/61388963:_____/13:00421956 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1021/jz4022238" target="_blank" >http://dx.doi.org/10.1021/jz4022238</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/jz4022238" target="_blank" >10.1021/jz4022238</a>

Result language
angličtina
Original language name
Effects of end-group termination on salting-out constants for triglycine
Original language description
Salting-out constants for triglycine were calculated for a series of Hofmeister salts using molecular dynamics simulations. Three variants of the peptide were considered with both termini capped, just the N-terminus capped, and without capping. The simulations were supported by NMR and FTIR measurements. The data provide strong evidence that previous experimental values of salting-out constants assigned to the fully capped peptide (as previously assumed) should have been assigned to the half-capped peptide instead. Therefore, these values cannot be used to directly establish Hofmeister ordering of ions at the peptide backbone because they are strongly influenced by interactions of the ions with the negatively charged C terminus.
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
—

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

Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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