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

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
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. 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. (en)
Title	Effects of end-group termination on salting-out constants for triglycine Effects of end-group termination on salting-out constants for triglycine (en)
skos:prefLabel	Effects of end-group termination on salting-out constants for triglycine Effects of end-group termination on salting-out constants for triglycine (en)
skos:notation	RIV/61388963:_____/13:00421956!RIV14-GA0-61388963
http://linked.open...avai/riv/aktivita	I P
http://linked.open...avai/riv/aktivity	I, P(GBP208/12/G016)
http://linked.open...iv/cisloPeriodika	23
http://linked.open...vai/riv/dodaniDat	2014
http://linked.open...aciTvurceVysledku	Jungwirth, Pavel Paterová, Jana
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Ústav organické chemie a biochemie AV ČR, v. v. i.
http://linked.open...dnocenehoVysledku	71935
http://linked.open...ai/riv/idVysledku	RIV/61388963:_____/13:00421956
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	ions; Hofmeister series; triglycine; NMR; molecular dynamics (en)
http://linked.open.../riv/klicoveSlovo	Hofmeister series triglycine ions NMR molecular dynamics
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[817C0DBFA2B1]
http://linked.open...i/riv/nazevZdroje	Journal of Physical Chemistry Letters
http://linked.open...in/vavai/riv/obor	CF
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	9 (xsd:int)
http://linked.open...vavai/riv/projekt	Controlling structure and function of biomolecules at the molecular scale: theory meets experiment
http://linked.open...UplatneniVysledku	2013
http://linked.open...v/svazekPeriodika	4
http://linked.open...iv/tvurceVysledku	Jungwirth, Pavel Cremer, P. S. Hilty, Ch. Rembert, K. B. Heyda, J. Hladílková, Jana Kurra, Y. Liu, W. R. Okur, H. I.
http://linked.open...ain/vavai/riv/wos	000328101000010
issn	1948-7185
number of pages	5 (xsd:int)
http://bibframe.org/vocab/doi	10.1021/jz4022238

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