Related ArticlesRealtime (31)P NMR Investigation on the Catalytic Behavior of the Enzyme Adenylate kinase in the Matrix of a Switchable Ionic Liquid.
ChemSusChem. 2015 Nov;8(22):3764-8
Authors: Rogne P, Sparrman T, Anugwom I, Mikkola JP, Wolf-Watz M
Abstract
The integration of highly efficient enzymatic catalysis with the solvation properties of ionic liquids for an environmentally friendly and efficient use of raw materials such as wood requires fundamental knowledge about the influence of relevant ionic liquids on enzymes. Switchable ionic liquids (SIL) are promising candidates for implementation of enzymatic treatments of raw materials. One industrially interesting SIL is constituted by monoethanol amine (MEA) and 1,8-diazabicyclo-[5.4.0]-undec-7-ene (DBU) formed with sulfur dioxide (SO2) as the coupling media (DBU-SO2-MEASIL). It has the ability to solubilize the matrix of lignocellulosic biomass while leaving the cellulose backbone intact. Using a novel (31)P NMR-based real-time assay we show that this SIL is compatible with enzymatic catalysis because a model enzyme, adenylate kinase, retains its activity in up to at least 25 wt % of DBU-SO2-MEASIL. Thus this SIL appears suitable for, for example, enzymatic degradation of hemicellulose.
NMR Study of Ion Dynamics and Charge Storage in Ionic Liquid Supercapacitors
NMR Study of Ion Dynamics and Charge Storage in Ionic Liquid Supercapacitors
Alexander C. Forse, John M. Griffin, Ce?line Merlet, Paul M. Bayley, Hao Wang, Patrice Simon and Clare P. Grey
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b03958/20150529/images/medium/ja-2015-03958k_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b03958
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ZZefmYGzFNI
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[NMR paper] A minor conformation of a lanthanide tag on adenylate kinase characterized by paramagnetic relaxation dispersion NMR spectroscopy.
A minor conformation of a lanthanide tag on adenylate kinase characterized by paramagnetic relaxation dispersion NMR spectroscopy.
A minor conformation of a lanthanide tag on adenylate kinase characterized by paramagnetic relaxation dispersion NMR spectroscopy.
J Biomol NMR. 2015 Jan 8;
Authors: Hass MA, Liu W, Agafonov RV, Otten R, Phung LA, Schilder JT, Kern D, Ubbink M
Abstract
NMR relaxation dispersion techniques provide a powerful method to study protein dynamics by characterizing lowly populated conformations that are in...
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01-08-2015 01:29 PM
A minor conformation of a lanthanide tag on adenylate kinase characterized by paramagnetic relaxation dispersion NMR spectroscopy
A minor conformation of a lanthanide tag on adenylate kinase characterized by paramagnetic relaxation dispersion NMR spectroscopy
Abstract
NMR relaxation dispersion techniques provide a powerful method to study protein dynamics by characterizing lowly populated conformations that are in dynamic exchange with the major state. Paramagnetic NMR is a versatile tool for investigating the structures and dynamics of proteins. These two techniques were combined here to measure accurate and precise pseudocontact shifts of a lowly populated conformation. This...
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[NMR paper] Nmr structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
Nmr structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
Related Articles Nmr structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
J Struct Biol. 2013 Nov 6;
Authors: Jaremko M, Jaremko L, Nowakowski M, Wojciechowski M, Szczepanowski RH, Panecka R, Zhukov I, Bochtler M, Ejchart A
Abstract
We report a high resolution NMR structure and (15)N relaxation studies of the first catalytic cysteine half-domain (FCCH) of the mouse ubiquitin-activating enzyme E1, together with...
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11-12-2013 03:52 PM
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
J Agric Food Chem. 2011 Jan 10;
Authors: Monogioudi E, Permi P, Filpponen I, Lienemann M, Li B, Argyropoulos D, Buchert J, Mattinen ML
Cross-linking of ?-casein by Trichoderma reesei tyrosinase (TrTyr) and Streptoverticillium mobaraense transglutaminase (Tgase) was analyzed by (31)P nuclear magnetic...
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[NMR paper] A novel view of domain flexibility in E. coli adenylate kinase based on structural mo
A novel view of domain flexibility in E. coli adenylate kinase based on structural mode-coupling (15)N NMR relaxation.
Related Articles A novel view of domain flexibility in E. coli adenylate kinase based on structural mode-coupling (15)N NMR relaxation.
J Mol Biol. 2002 Jan 11;315(2):155-70
Authors: Tugarinov V, Shapiro YE, Liang Z, Freed JH, Meirovitch E
Adenylate kinase from Escherichia coli (AKeco), consisting of a single 23.6 kDa polypeptide chain folded into domains CORE, AMPbd and LID, catalyzes the reaction AMP+ATP-->2ADP. In the...
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[NMR paper] Complexes of yeast adenylate kinase and nucleotides investigated by 1H NMR.
Complexes of yeast adenylate kinase and nucleotides investigated by 1H NMR.
Related Articles Complexes of yeast adenylate kinase and nucleotides investigated by 1H NMR.
Biochemistry. 1991 Apr 30;30(17):4137-42
Authors: Vetter IR, Konrad M, Rösch P
The role of one of the histidine residues present in many adenylate kinases (H36 in the porcine cytosolic enzyme) is highly disputed. We thus studied the yeast enzyme (AKye) containing this His residue. AKye is highly homologous to the Escherichia coli enzyme (AKec), a protein that is already well...
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[NMR paper] Complexes of Escherichia coli adenylate kinase and nucleotides: 1H NMR studies of the
Complexes of Escherichia coli adenylate kinase and nucleotides: 1H NMR studies of the nucleotide sites in solution.
Related Articles Complexes of Escherichia coli adenylate kinase and nucleotides: 1H NMR studies of the nucleotide sites in solution.
Biochemistry. 1990 Aug 14;29(32):7459-67
Authors: Vetter IR, Reinstein J, Rösch P
One- and two-dimensional nuclear magnetic resonance (NMR) studies, in particular substrate--protein nuclear Overhauser effect (NOESY) measurements, as well as nucleotide and P1,P5-bis-(5'-adenosyl) pentaphosphate...
Realtime (31)P NMR Investigation on the Catalytic Behavior of the Enzyme Adenylate kinase in the Matrix of a Switchable Ionic Liquid.
Linear Mode
