Reversal of the Hofmeister Series: Specific Ion Effects on Peptides

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F13%3A00395118" target="_blank" >RIV/61388963:_____/13:00395118 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1021/jp405683s" target="_blank" >http://dx.doi.org/10.1021/jp405683s</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/jp405683s" target="_blank" >10.1021/jp405683s</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Reversal of the Hofmeister Series: Specific Ion Effects on Peptides

Popis výsledku v původním jazyce

Ion-specific effects On salting-in and salting-out of proteins, protein denaturation, as well as enzymatic activity are typically rationalized in terms of the Hofmeister Here, we demonstrate by means of NMR spectroscopy and, molecular dynamics simulations that the traditional explanation of the Hofmeister ordering of ions in term of their bulk hydration properties is inadequate. Using triglycine as a model system, we show that the Hofmeister series for anions changes from a direct to a reversed series upon uncapping the N- terminus. Weakly hydrated anions, such as iodide and thio cyanate, interact with the peptide bond; while strongly hydrated anions like sulfate are repelled from it. In Contrast reversed order in interactions, of anions is observed atthe positively charged, uncapped N-terminus, and by analogy, this should also be the case at side chains of positively,Charged amino These results demonstrate that the specific chemical and physical properties, of peptides and proteins p

Název v anglickém jazyce

Reversal of the Hofmeister Series: Specific Ion Effects on Peptides

Popis výsledku anglicky

Ion-specific effects On salting-in and salting-out of proteins, protein denaturation, as well as enzymatic activity are typically rationalized in terms of the Hofmeister Here, we demonstrate by means of NMR spectroscopy and, molecular dynamics simulations that the traditional explanation of the Hofmeister ordering of ions in term of their bulk hydration properties is inadequate. Using triglycine as a model system, we show that the Hofmeister series for anions changes from a direct to a reversed series upon uncapping the N- terminus. Weakly hydrated anions, such as iodide and thio cyanate, interact with the peptide bond; while strongly hydrated anions like sulfate are repelled from it. In Contrast reversed order in interactions, of anions is observed atthe positively charged, uncapped N-terminus, and by analogy, this should also be the case at side chains of positively,Charged amino These results demonstrate that the specific chemical and physical properties, of peptides and proteins p

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

<a href="/cs/project/GBP208%2F12%2FG016" target="_blank" >GBP208/12/G016: Řízení struktury a funkce biomolekul na molekulové úrovni: souhra teorie a experimentu</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Physical Chemistry B

ISSN

1520-6106

e-ISSN

—

Svazek periodika

117

Číslo periodika v rámci svazku

27

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

8150-8158

Kód UT WoS článku

000321884100011

EID výsledku v databázi Scopus

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