| Hauptseite > Publikationsdatenbank > The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions: structure, dynamics, and enzyme activity > print |
| 001 | 15317 | ||
| 005 | 20240619092059.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:21416312 |
| 024 | 7 | _ | |2 DOI |a 10.1007/s00249-011-0689-0 |
| 024 | 7 | _ | |2 WOS |a WOS:000290331400006 |
| 024 | 7 | _ | |2 MLZ |a WellertTKRLHGBSSH2011 |
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| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Wellert, S. |b 0 |
| 245 | _ | _ | |a The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions: structure, dynamics, and enzyme activity |
| 260 | _ | _ | |a Berlin |b Springer |c 2011 |
| 300 | _ | _ | |a 761 - 774 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 10441 |a European Biophysics Journal : with Biophysics Letters |v 40 |x 0175-7571 |y 6 |
| 500 | _ | _ | |a J.G. and M.M.B. were supported by the German Ministry of Defense under contract E/UR3G/6G115/6A801. T. H., R. S., C. S. also were financed by the German Ministry of Defense (Contracts E/E590/9Z004/5F159 and E/E590/8Z002/4F170). The SANS experiments were supported by the European Union through the NMI3 program. We are grateful to the Laboratoire Leon Brillouin and the Julich Center for Neutron Scattering at the FRM II for providing beamtime. |
| 520 | _ | _ | |a The enzyme diisopropyl fluorophosphatase (DFPase) from the squid Loligo vulgaris is of great interest because of its ability to catalyze the hydrolysis of highly toxic organophosphates. In this work, the enzyme structure in solution (native state) was studied by use of different scattering methods. The results are compared with those from hydrodynamic model calculations based on the DFPase crystal structure. Bicontinuous microemulsions made of sugar surfactants are discussed as host systems for the DFPase. The microemulsion remains stable in the presence of the enzyme, which is shown by means of scattering experiments. Moreover, activity assays reveal that the DFPase still has high activity in this complex reaction medium. To complement the scattering experiments cryo-SEM was also employed to study the microemulsion structure. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK505 |2 G:(DE-HGF) |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |c P45 |x 0 |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK415 |2 G:(DE-HGF) |a Großgeräte für die Forschung mit Photonen, Neutronen und Ionen (PNI) |c P55 |x 1 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Animals |
| 650 | _ | 2 | |2 MeSH |a Carbohydrates: chemistry |
| 650 | _ | 2 | |2 MeSH |a Carbohydrates: pharmacology |
| 650 | _ | 2 | |2 MeSH |a Emulsions |
| 650 | _ | 2 | |2 MeSH |a Loligo: enzymology |
| 650 | _ | 2 | |2 MeSH |a Loligo: metabolism |
| 650 | _ | 2 | |2 MeSH |a Microscopy, Electron, Scanning |
| 650 | _ | 2 | |2 MeSH |a Neutron Diffraction |
| 650 | _ | 2 | |2 MeSH |a Phosphoric Triester Hydrolases: analysis |
| 650 | _ | 2 | |2 MeSH |a Phosphoric Triester Hydrolases: chemistry |
| 650 | _ | 2 | |2 MeSH |a Phosphoric Triester Hydrolases: metabolism |
| 650 | _ | 2 | |2 MeSH |a Scattering, Small Angle |
| 650 | _ | 2 | |2 MeSH |a Solutions: chemistry |
| 650 | _ | 2 | |2 MeSH |a Surface-Active Agents: chemistry |
| 650 | _ | 2 | |2 MeSH |a Surface-Active Agents: pharmacology |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Carbohydrates |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Emulsions |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Solutions |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Surface-Active Agents |
| 650 | _ | 7 | |0 EC 3.1.8.- |2 NLM Chemicals |a Phosphoric Triester Hydrolases |
| 650 | _ | 7 | |0 EC 3.1.8.2 |2 NLM Chemicals |a diisopropyl-fluorophosphatase |
| 650 | _ | 7 | |2 WoSType |a J |
| 650 | 2 | 7 | |0 V:(DE-MLZ)SciArea-160 |2 V:(DE-HGF) |a Biology |x 0 |
| 650 | 1 | 7 | |a Health and Life |0 V:(DE-MLZ)GC-130-2016 |2 V:(DE-HGF) |x 1 |
| 650 | 1 | 7 | |a Health and Life |0 V:(DE-MLZ)GC-130-1 |2 V:(DE-HGF) |x 0 |
| 653 | 2 | 0 | |2 Author |a Dynamic light scattering |
| 653 | 2 | 0 | |2 Author |a Neutron spin echo |
| 653 | 2 | 0 | |2 Author |a Microemulsion |
| 653 | 2 | 0 | |2 Author |a Enzyme catalysis |
| 653 | 2 | 0 | |2 Author |a SANS |
| 653 | 2 | 0 | |2 Author |a Protein structure |
| 693 | _ | _ | |0 EXP:(DE-MLZ)J-NSE-20140101 |1 EXP:(DE-MLZ)FRMII-20140101 |5 EXP:(DE-MLZ)J-NSE-20140101 |6 EXP:(DE-MLZ)NL2ao-20140101 |a Forschungs-Neutronenquelle Heinz Maier-Leibnitz |e J-NSE: Neutron spin-echo spectrometer |f NL2ao |x 0 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Tiersch, B. |b 1 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Koetz, J. |b 2 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Richardt, A. |b 3 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Lapp, A. |b 4 |
| 700 | 1 | _ | |0 P:(DE-Juel1)130718 |a Holderer, O. |b 5 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Gäb, J. |b 6 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Blum, M.-M. |b 7 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Schulreich, C. |b 8 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Stehle, R. |b 9 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Hellweg, T. |b 10 |
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| 856 | 7 | _ | |u http://dx.doi.org/10.1007/s00249-011-0689-0 |
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