Lyophilized products were dissolved to 3−10 mM in 50 mM potassium phosphate buffer (pD 7.9) in a total volume of 600 μL and transferred to a 5 mm high-precision NMR sample tube. They were analyzed using a Varian INOVA 500-MHz NMR spectrometer (Agilent Technologies). The VNMRJ 2.2D software was used for measurements. 1H-NMR spectra (499.98 MHz) were measured on a 5 mm indirect detection PFG probe. Standard pre-saturation sequence was used: relaxation delay 2 s; 908 proton pulse; 2.048 s acquisition time; spectral width 8 kHz; number of points 32,000 13C NMR spectra (125.71 MHz). Standard pre-saturation sequence was used: relaxation delay 2 s; 908 proton pulse; 2.048 s acquisition time; spectral width 8 kHz; number of points 32 k. MNova 12.0.3 (Mestrelab Research S.L. Bajo, Santiago de Compostela, Spain) was used for data processing and analysis (Supplementary Figs. 10 –29 ). Recorded spectra were in good agreement with published data75 (link).
Mnova 12
Manufactured by Mestrelab Research
Sourced in Spain
MNova 12.0.3 is a software application developed by Mestrelab Research for the analysis and processing of nuclear magnetic resonance (NMR) data. It provides a comprehensive set of tools for tasks such as viewing, processing, and analyzing NMR spectra.
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4 protocols using mnova 12
1
NMR Characterization of Lyophilized Products
2
NMR Analysis of Marine Extracts
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Aliquots from each extract in Section 4.3 dried by N2 flow were dissolved in 200 µL of CD3OD, and 50 µL of this sample was added to a 1.7 mm NMR SampleJet (Bruker) NMR tube. NMR data were acquired with a Bruker Avance III 600 MHz spectrometer equipped with a 1.7 mm cryoprobe. HSQC spectra were acquired using the Bruker pulse sequence “hsqcedetgpsisp2.3” modified to include a DIPSI-2 spinlock in the relaxation delay for the ASAP protocol [22 (link)]. Chemical shifts were referenced using the corresponding solvent signals (δH 3.31 and δC 49.0 for CD3OD). The NMR spectra were processed using Mnova 12.0.3 (Mestrelab Research) or TopSpin 3.6 (Bruker Biospin).
3
NMR Analysis of Funerary Pigments and Resins
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The measurements were conducted with the s2pul sequence. The relaxation delay was 1.0 s, and the acquisition time was 3.0 s. The profiles of the funerary pigment samples were the result of 15,000 scans, while the resin and triterpenoid profiles were obtained by 64 scans with data collected into 64k data points. Each free induction decay (FID) was zero-filled to 128k data points. Prior to Fourier transformation, a Gaussian window function with a line broadening factor of 0.2 Hz was applied. The resulting spectra were manually phased, and baseline corrected using MNova 12.0 (Mestrelab Research S.L.).
4
NMR Spectroscopy Protocols for Chemical Analysis
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The following instruments were used to acquire NMR spectra. Spectra are shown in Supporting information 3.
Instrument 1: 1 H (600 MHz) and 13 C (150 MHz, referenced to the NMR solvent peak) spectra were recorded on a Bruker AV600 NMR spectrometer, in the solvent stated, using a 5 mm TCI cryoprobe. 1 (link) H NMR spectra were referenced to an external TMS reference at δ = 0 ppm.
Instrument 2: 1 H NMR (400 MHz), and 13 C NMR (100 MHz) spectra were recorded on a Bruker Avance III 400 MHz spectrometer performed at 293K in the solvent stated. Chemical shifts (δ) are given in parts per million (ppm) where TMS singlet is set at 0 ppm. Coupling constants are given as absolute values in Hertz.
Instrument 3: The 1 H (60 MHz) spectrum was recorded on a NMReady-60e benchtop NMR spectrometer (Nanalysis Corp, Calgary, Canada) using the following conditions: 5 mm NMR tube; 4096 scans at 32°C; pulse sequence, 1DPULSEACQUIRE. Data was processed in MNova 12.0 (Mestrelab Research, Santiago de Compostela, Spain).
Instrument 1: 1 H (600 MHz) and 13 C (150 MHz, referenced to the NMR solvent peak) spectra were recorded on a Bruker AV600 NMR spectrometer, in the solvent stated, using a 5 mm TCI cryoprobe. 1 (link) H NMR spectra were referenced to an external TMS reference at δ = 0 ppm.
Instrument 2: 1 H NMR (400 MHz), and 13 C NMR (100 MHz) spectra were recorded on a Bruker Avance III 400 MHz spectrometer performed at 293K in the solvent stated. Chemical shifts (δ) are given in parts per million (ppm) where TMS singlet is set at 0 ppm. Coupling constants are given as absolute values in Hertz.
Instrument 3: The 1 H (60 MHz) spectrum was recorded on a NMReady-60e benchtop NMR spectrometer (Nanalysis Corp, Calgary, Canada) using the following conditions: 5 mm NMR tube; 4096 scans at 32°C; pulse sequence, 1DPULSEACQUIRE. Data was processed in MNova 12.0 (Mestrelab Research, Santiago de Compostela, Spain).
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