Interaction of Organic Solvents with Protein Structures at Protein-Solvent Interface

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F13%3A00065827" target="_blank" >RIV/00216224:14310/13:00065827 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67179843:_____/13:00381609 RIV/60076658:12310/13:43883858 RIV/00159816:_____/13:00060713

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s00894-012-1507-z" target="_blank" >http://dx.doi.org/10.1007/s00894-012-1507-z</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00894-012-1507-z" target="_blank" >10.1007/s00894-012-1507-z</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Interaction of Organic Solvents with Protein Structures at Protein-Solvent Interface

Popis výsledku v původním jazyce

The effect of non-denaturing concentrations of three different organic solvents, formamide, acetone and isopropanol, on the structure of haloalkane dehalogenases DhaA, LinB, and DbjA at the protein-solvent interface was studied using molecular dynamics simulations. Analysis of B-factors revealed that the presence of a given organic solvent mainly affects the dynamical behavior of the specificity-determining cap domain, with the exception of DbjA in acetone. Orientation of organic solvent molecules on the protein surface during the simulations was clearly dependent on their interaction with hydrophobic or hydrophilic surface patches, and the simulations suggest that the behavior of studied organic solvents in the vicinity of hyrophobic patches on the surface is similar to the air/water interface. DbjA was the only dimeric enzyme among studied haloalkane dehalogenases and provided an opportunity to explore effects of organic solvents on the quaternary structure.

Název v anglickém jazyce

Interaction of Organic Solvents with Protein Structures at Protein-Solvent Interface

Popis výsledku anglicky

The effect of non-denaturing concentrations of three different organic solvents, formamide, acetone and isopropanol, on the structure of haloalkane dehalogenases DhaA, LinB, and DbjA at the protein-solvent interface was studied using molecular dynamics simulations. Analysis of B-factors revealed that the presence of a given organic solvent mainly affects the dynamical behavior of the specificity-determining cap domain, with the exception of DbjA in acetone. Orientation of organic solvent molecules on the protein surface during the simulations was clearly dependent on their interaction with hydrophobic or hydrophilic surface patches, and the simulations suggest that the behavior of studied organic solvents in the vicinity of hyrophobic patches on the surface is similar to the air/water interface. DbjA was the only dimeric enzyme among studied haloalkane dehalogenases and provided an opportunity to explore effects of organic solvents on the quaternary structure.

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

Journal of Molecular Modeling

ISSN

1610-2940

e-ISSN

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Svazek periodika

19

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

4701-4711

Kód UT WoS článku

000326193200010

EID výsledku v databázi Scopus

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