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https://www.selleckchem.com/products/nvp-tnks656.html Reliable measurement of the binding kinetics of low molecular weight analytes to their targets is still a challenging task. Often, the introduction of labels is simply impossible in such measurements, and the application of label-free methods is the only reliable choice. By measuring the binding kinetics of Ni(II) ions to genetically modified flagellin layers, we demonstrate that (1) Grating-Coupled Interferometry (GCI) is well suited to resolve the binding of ions, even at very low protein immobilization levels; (2) it supplies high quality kinetic data from which the number and strength of available binding sites can be determined, and (3) the rate constants of the binding events can also be obtained with high accuracy. Experiments were performed using a flagellin variant incorporating the C-terminal domain of the nickel-responsive transcription factor NikR. GCI results were compared to affinity data from titration calorimetry. We found that besides the low-affinity binding sites characterized by a micromolar dissociation constant (Kd), tetrameric FliC-NikRC molecules possess high-affinity binding sites with Kd values in the nanomolar range. GCI enabled us to obtain real-time kinetic data for the specific binding of an analyte with molar mass as low as 59 Da, even at signals lower than 1 pg/mm2.Large ignimbrites are the product of devastating explosive eruptions that have repeatedly impacted climate and life on global scale. The assemblage of vertical and lateral lithofacies variations within an ignimbrite sheet, its internal architecture, may help to determine how the parental pyroclastic current evolves in time and space. The 39 ka Campanian Ignimbrite eruption, vented from Campi Flegrei caldera, laid down a thick ignimbrite over an area of thousands of km2. A detailed reconstruction of the vertical and lateral variation of the seven lithofacies recognised in the ignimbrite medial sequence constrains the beha

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