Interaction of organic solvents with protein structures at protein-solvent interface
Jazyk angličtina Země Německo Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- 2-propanol chemie farmakologie MeSH
- aceton chemie farmakologie MeSH
- formamidy chemie farmakologie MeSH
- hydrofobní a hydrofilní interakce MeSH
- hydrolasy chemie MeSH
- krystalografie rentgenová MeSH
- kvarterní struktura proteinů účinky léků MeSH
- molekulární modely MeSH
- rozpouštědla chemie MeSH
- simulace molekulární dynamiky MeSH
- terciární struktura proteinů účinky léků MeSH
- voda chemie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- 2-propanol MeSH
- aceton MeSH
- formamide MeSH Prohlížeč
- formamidy MeSH
- haloalkane dehalogenase MeSH Prohlížeč
- hydrolasy MeSH
- rozpouštědla MeSH
- voda MeSH
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. Penetration and trapping of organic solvents in the network of interactions between both monomers depends on the physico-chemical properties of the organic solvents. Consequently, both monomers of this enzyme oscillate differently in different organic solvents. With the exception of LinB in acetone, the structures of studied enzymes were stabilized in water-miscible organic solvents.
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