SAR302503 br Experimental design materials and methods br Da

Experimental design, materials and methods
Data The data include table and figures, which help analyze the phosphorylated peptides and DSP. The peptic peptides detected by LC FTICR MS after 5min SAR302503 of natural ovalbumin as control are listed in Supplementary Table 1. Compared with the control, the phosphorylated peptides were directly determined from the mass increases of 79.9663 or its multiples. From these data, we exemplified the mass spectrometry to identify and calculate the DSP of each phosphorylated peptide (Figs. S1–S3 and Fig. 1). Here, we also exemplified the DSP calculation method from the peak abundance (Fig. 2).
Experimental design, materials and methods
Acknowledgments This work was supported by the National High Technology Research and Development Program of China (863 Program, No. 2013AA102205), National Natural Science Foundation of China (No. 31560458) and the Research Foundation for Young Scientists of State Key Laboratory of Food Science and Technology, Nanchang University, China (No. SKLF-QN-201511).
Data The data henceforth described refers to the 1H-NMR experiments of three coumarins, Aesculetin, 4-Methylumbelliferone, and umbelliferone, in deuterated acetone. The data disclosed regards the 1H-NMR experiments conducted with 4-Methylumbelliferone (Fig. 1), umbelliferone (fig. 2), and Aesculetin (Fig. 3), in deuterated acetone. This data may be helpful for those who intend to compare this data with other from molecules containing the same or related coumarins scaffolds. Table 1 lists all the peaks and their respective intensities.
Experimental design, materials, and methods The compounds were subjected to 1H-NMR measurements. The experiments were performed on a Bruker Avance 400 liquid NMR spectrometer, operating at 400MHz. Detection temperature was set at 25oC. The samples were loaded in a 5mm NMR tube. The solvent peak was calibrated according to Gottlieb et al. [1].
Data Data reported in the following are distinguished in three sub-sections: NMR analysis; computational methods; peptide design. In the first we report the proton chemical shifts of MTP1 and MTP2 peptides in DMSO and TFE/H2O 1:1 (Tables 1–4), together with the diagrams of the most relevant NOE effects (Figs. 1 and 2) and the deviations of the αCH protons from random coil values (Figs. 3 and 4). Next, we show the structural statistics of the molecular model calculations for MTP1 and MTP2 (Tables 5 and 6). Finally, the computed parameters from the computational tools used in the peptide designing.
Experimental design, materials and methods
Acknowledgments This research was supported by PON-RICERCA E COMPETITIVITÀ 2007-2013, MAREA (Materiali Avanzati per il comparto agroalimentare- PON03PE_00106_1; Regione Campania POR Campania FESR 2007-2013 - O.O. 2.1 - Rete delle Biotecnologie in Campania (FarmaBioNet project))\"; EUROTRANSBIO transnational project \"SUPPLE, Sustainable plant-based production of extremozymes\" F/0004/02/X29.
Data
Experimental design, materials and methods The various chemical components were analyzed and identified by GC–MS analysis as previously described [1]. Data was gathered with Chem station. (Table 1).
Acknowledgements This work was financially supported by Govan Mbeki Research & Development Council (GMRDC).
Data The data here presented describes the synthesis procedure and analysis of epigallocatechin-(4β→8)-epigallocatechin gallate (EGC-EGCG), a prodelphinidin dimer (Fig. 1) [1]. The synthesis procedure starts from the two constitutive monomers: (-)-Epigallocatechin (EGC) and (-)-epigallocatechin gallate (EGCG), and includes a new approach to the removal of the protecting groups.
Experimental design, materials and methods
Acknowledgements Natércia Teixeira, gratefully acknowledge a post-doctoral scholarship grant (FOOD_RL1_PHD_QUINOA_01_02), under the financial support with the reference UID/QUI/50006/2013-POCI/01/0145/FEDER/007265 and from FCT/MEC through national funds and co-financed by FEDER, under the Partnership Agreement PT2020