Like-charged protein-polyelectrolyte complexation driven by charge patches
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F15%3A43899669" target="_blank" >RIV/60461373:22340/15:43899669 - isvavai.cz</a>
Výsledek na webu
<a href="http://scitation.aip.org/content/aip/journal/jcp/143/6/10.1063/1.4928078" target="_blank" >http://scitation.aip.org/content/aip/journal/jcp/143/6/10.1063/1.4928078</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1063/1.4928078" target="_blank" >10.1063/1.4928078</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Like-charged protein-polyelectrolyte complexation driven by charge patches
Popis výsledku v původním jazyce
We study the pair complexation of a single, highly charged polyelectrolyte (PE) chain (of 25 or 50 monomers) with like-charged patchy protein models (CPPMs) by means of implicit-solvent, explicit-salt Langevin dynamics computer simulations. Our previously introduced set of CPPMs embraces well-defined zero-, one-, and two-patched spherical globules each of the same net charge and (nanometer) size with mono-and multipole moments comparable to those of globular proteins with similar size. We observe largebinding affinities between the CPPM and the like-charged PE in the tens of the thermal energy, k(B)T, that are favored by decreasing salt concentration and increasing charge of the patch(es). Our systematic analysis shows a clear correlation between thedistance-resolved potentials of mean force, the number of ions released from the PE, and CPPM orientation effects. In particular, we find a novel two-site binding behavior for PEs in the case of two-patched CPPMs, where intermediate metas
Název v anglickém jazyce
Like-charged protein-polyelectrolyte complexation driven by charge patches
Popis výsledku anglicky
We study the pair complexation of a single, highly charged polyelectrolyte (PE) chain (of 25 or 50 monomers) with like-charged patchy protein models (CPPMs) by means of implicit-solvent, explicit-salt Langevin dynamics computer simulations. Our previously introduced set of CPPMs embraces well-defined zero-, one-, and two-patched spherical globules each of the same net charge and (nanometer) size with mono-and multipole moments comparable to those of globular proteins with similar size. We observe largebinding affinities between the CPPM and the like-charged PE in the tens of the thermal energy, k(B)T, that are favored by decreasing salt concentration and increasing charge of the patch(es). Our systematic analysis shows a clear correlation between thedistance-resolved potentials of mean force, the number of ions released from the PE, and CPPM orientation effects. In particular, we find a novel two-site binding behavior for PEs in the case of two-patched CPPMs, where intermediate metas
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CF - Fyzikální chemie a teoretická chemie
OECD FORD obor
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Návaznosti výsledku
Projekt
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Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2015
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Journal of Chemical Physics
ISSN
0021-9606
e-ISSN
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Svazek periodika
143
Číslo periodika v rámci svazku
6
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
12
Strana od-do
064905
Kód UT WoS článku
000359799600046
EID výsledku v databázi Scopus
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