How simple is too simple? Computational perspective on importance of second-shell environment for metal-ion selectivity

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F15%3A00445329" target="_blank" >RIV/61388963:_____/15:00445329 - isvavai.cz</a>

Výsledek na webu

<a href="http://pubs.rsc.org/en/content/articlepdf/2015/cp/c4cp04876h" target="_blank" >http://pubs.rsc.org/en/content/articlepdf/2015/cp/c4cp04876h</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/c4cp04876h" target="_blank" >10.1039/c4cp04876h</a>

Jazyk výsledku

angličtina

Název v původním jazyce

How simple is too simple? Computational perspective on importance of second-shell environment for metal-ion selectivity

Popis výsledku v původním jazyce

The metal-ion selectivity in biomolecules represents one of the most important phenomena in bioinorganic chemistry. The open question to what extent is the selectivity in the complex bioinorganic structures such as metallopeptides determined by the first-shell ligands of the metal ion is answered herein using six model peptides complexed with the set of divalent metal ions (Mn2+, Fe2+, Co2+, Ni2+, Cu2+, Zn2+, Cd2+, and Hg2+) and their various first-shell representations. By calculating the differences among the free energies of complexation of metal ions in these peptides and their model (truncated) systems it is quantitatively shown that the definition of the first shell is paramount to this discussion and revolves around the chemical nature of the binding site. Despite the vast conceivable diversity of peptidic structures, that suggest certain fluidity of this definition, major contributing factors are identified and assessed based on their importance for capturing metal-ion selectiv

Název v anglickém jazyce

How simple is too simple? Computational perspective on importance of second-shell environment for metal-ion selectivity

Popis výsledku anglicky

The metal-ion selectivity in biomolecules represents one of the most important phenomena in bioinorganic chemistry. The open question to what extent is the selectivity in the complex bioinorganic structures such as metallopeptides determined by the first-shell ligands of the metal ion is answered herein using six model peptides complexed with the set of divalent metal ions (Mn2+, Fe2+, Co2+, Ni2+, Cu2+, Zn2+, Cd2+, and Hg2+) and their various first-shell representations. By calculating the differences among the free energies of complexation of metal ions in these peptides and their model (truncated) systems it is quantitatively shown that the definition of the first shell is paramount to this discussion and revolves around the chemical nature of the binding site. Despite the vast conceivable diversity of peptidic structures, that suggest certain fluidity of this definition, major contributing factors are identified and assessed based on their importance for capturing metal-ion selectiv

Druh

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

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

—

Projekt

<a href="/cs/project/GA14-31419S" target="_blank" >GA14-31419S: Počítačový design minimalistických metalopeptidů jako cesta k rozluštění katalytické účinnosti metaloproteinů</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Physical Chemistry Chemical Physics

ISSN

1463-9076

e-ISSN

—

Svazek periodika

17

Číslo periodika v rámci svazku

22

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

12

Strana od-do

14393-14404

Kód UT WoS článku

000355633400014

EID výsledku v databázi Scopus

2-s2.0-84930667546