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024 7 _ |2 pmid
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024 7 _ |2 DOI
|a 10.1007/s00249-011-0689-0
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|a WellertTKRLHGBSSH2011
037 _ _ |a PreJuSER-15317
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
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336 7 _ |a Journal Article
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336 7 _ |a ARTICLE
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336 7 _ |a JOURNAL_ARTICLE
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336 7 _ |a article
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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.
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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
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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
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|5 EXP:(DE-MLZ)J-NSE-20140101
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|a Forschungs-Neutronenquelle Heinz Maier-Leibnitz
|e J-NSE: Neutron spin-echo spectrometer
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700 1 _ |0 P:(DE-HGF)0
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700 1 _ |0 P:(DE-HGF)0
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700 1 _ |0 P:(DE-Juel1)130718
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700 1 _ |0 P:(DE-HGF)0
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700 1 _ |0 P:(DE-HGF)0
|a Blum, M.-M.
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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.
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|a 10.1007/s00249-011-0689-0
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|p 761 - 774
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|t European biophysics journal
|v 40
|x 0175-7571
|y 2011
856 7 _ |u http://dx.doi.org/10.1007/s00249-011-0689-0
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914 1 _ |y 2011
915 _ _ |0 StatID:(DE-HGF)0010
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