Number of the records: 1  

Stabilization of Haloalkane Dehalogenase Structure by Interfacial Interaction with Ionic Liquids

  1. 1.
    0547429 - MBÚ 2022 RIV CH eng J - Journal Article
    Shaposhnikova, Anastasiia - Kutý, M. - Chaloupková, R. - Damborský, J. - Smatanová, I.K. - Minofar, Babak - Prudnikova, T.
    Stabilization of Haloalkane Dehalogenase Structure by Interfacial Interaction with Ionic Liquids.
    Crystals. Roč. 11, č. 9 (2021), č. článku 1052. ISSN 2073-4352. E-ISSN 2073-4352
    R&D Projects: GA MŠMT(CZ) LM2015047
    Research Infrastructure: e-INFRA CZ - 90140; RECETOX RI - 90121
    Institutional support: RVO:61388971
    Keywords : haloalkane dehalogenase (HLD) * ionic liquids (ILs) * molecular dynamics (MD) simulations * protein stability * 2-hydroxyethylammonium acetate ([ETA][ACC]) * 1-butyl-3-methylimidazolium methyl sulfate ([EMIM][CHS])
    OECD category: Biophysics
    Impact factor: 2.670, year: 2021
    Method of publishing: Open access
    https://www.mdpi.com/2073-4352/11/9/1052

    Ionic liquids attracted interest as green alternatives to replace conventional organic solvents in protein stability studies. They can play an important role in the stabilization of enzymes such as haloalkane dehalogenases that are used for biodegradation of warfare agents and halogenated environmental pollutants. Three-dimensional crystals of haloalkane dehalogenase variant DhaA80 (T148L+G171Q+A172V+C176F) from Rhodococcus rhodochrous NCIMB 13064 were grown and soaked with the solutions of 2-hydroxyethylammonium acetate and 1-butyl-3-methylimidazolium methyl sulfate. The objective was to study the structural basis of the interactions between the ionic liquids and the protein. The diffraction data were collected for the 1.25 angstrom resolution for 2-hydroxyethylammonium acetate and 1.75 angstrom resolution for 1-butyl-3-methylimidazolium methyl sulfate. The structures were used for molecular dynamics simulations to study the interactions of DhaA80 with the ionic liquids. The findings provide coherent evidence that ionic liquids strengthen both the secondary and tertiary protein structure due to extensive hydrogen bond interactions.
    Permanent Link: http://hdl.handle.net/11104/0323664

     
     
Number of the records: 1  

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.