Interaction of Organic Solvents with Protein Structures at Protein-Solvent Interface
The result's identifiers
Result code in 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>
Alternative codes found
RIV/67179843:_____/13:00381609 RIV/60076658:12310/13:43883858 RIV/00159816:_____/13:00060713
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Interaction of Organic Solvents with Protein Structures at Protein-Solvent Interface
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Molecular Modeling
ISSN
1610-2940
e-ISSN
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Volume of the periodical
19
Issue of the periodical within the volume
11
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
4701-4711
UT code for WoS article
000326193200010
EID of the result in the Scopus database
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