Mnova

Manufactured by Mestrelab Research

Sourced in Spain, United States

MNova is a software solution developed by Mestrelab Research for the analysis and processing of nuclear magnetic resonance (NMR) data. The core function of MNova is to provide users with tools for the visualization, manipulation, and interpretation of NMR spectra.

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Lab products found in correlation

Matlab, by MathWorks (5 mentions) Avance spectrometer, by Bruker (3 mentions) Topspin, by Bruker (2 mentions) Pulsar low field spectrometer, by Oxford Instruments (2 mentions) Dd2 600 mhz nmr spectrometer, by Agilent Technologies (2 mentions) Origin 2019, by OriginLab (2 mentions) Inova spectrometer, by Agilent Technologies (2 mentions) 2 13c pyruvic acid, by Merck Group (1 mentions) 1 13c glucose, by Merck Group (1 mentions) 3 13c glutamine, by Merck Group (1 mentions) Hypersense dnp polarizer, by Oxford Instruments (1 mentions) 5 mm tci cryoprobe, by Bruker (1 mentions) Dextran sulfate sodium (dss), by Cambridge Isotopes (1 mentions) Hepes d18, by Cambridge Isotopes (1 mentions) Vnmrj, by Agilent Technologies (1 mentions) Ecs 400, by JEOL (1 mentions) Avance 400 mhz, by Bruker (1 mentions) Rotary evaporator, by Büchi (1 mentions) Avance 600, by Bruker (1 mentions) Nycodenz, by Sartorius (1 mentions)

Close spelling variants of this product

MNova 12.0.3 MestreNova (Mnova) Mnova NMR Mnova software 9.0 Mnova NMR software package MNova 6.0.2 Mnova 11 MNova 9.0 MNova v 10.0 MestReNova (Mnova 12.0,

52 protocols using mnova

DHA Identification in Aerosol Samples

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¹H NMR spectra were obtained on a Bruker^® 400 MHz AVANCE II+ spectrometer, with a 30° pulse angle, a 60 s relaxation delay, and 256 acquisitions. Data were processed and analyzed by MNova^® (Mestrelab Research, S.L., Santiago de Compostela, Spain); integrations were performed using MNova’s^® global spectrum deconvolution (GSD) algorithm. To verify the presence of DHA within the collected aerosol, each sample was spiked with a minute amount of DHA standard. This standard was prepared by dissolving solid DHA dimer in DMSO-d₆ to a concentration of 1.4 M. DHA was allowed to monomerize in DMSO-d₆ solution for 3 days before use.

Vreeke S., Korzun T., Luo W., Jensen R.P., Peyton D.H, & Strongin R.M. (2018). Dihydroxyacetone levels in electronic cigarettes: Wick temperature and toxin formation. Aerosol science and technology : the journal of the American Association for Aerosol Research, 52(4), 370-376.

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Multinuclear MRS of Cell Cultures

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U87 and NHA cells were grown on beads, BT142 neurospheres were encapsulated in agarose, and all MRS studies were performed using an MR-compatible cell perfusion system as described (29 (link)-31 (link)). All studies were performed on a 500MHz INOVA spectrometer (Agilent Technologies). For ¹³C-MRS studies glucose or glutamine in the medium were replaced with 5mM 1-¹³C-glucose or 2mM 3-¹³C-glutamine (Sigma-Aldrich) and spectra acquired using 60° flip angle (FA), 6s repetition time (TR) and 15min acquisition time. For hyperpolarized ¹³C-MRS, 2-¹³C-pyruvic acid (Sigma-Aldrich) was hyperpolarized using the Hypersense DNP polarizer (Oxford Instruments), injected into the perfusion system to a final concentration of 5mM pyruvate, and dynamic sets of ¹³C-MRS spectra acquired using 5° FA and 3s TR over 300s. All peak integrals were quantified using Mnova (Mestrelab Research). For thermally polarized ¹³C-MRS peaks, were normalized to cell number and initial ¹³C-substrate concentrations. For hyperpolarized ¹³C-MRS studies, total glutamate signal was normalized to total pyruvate signal and cell number.

Izquierdo-Garcia J.L., Viswanath P., Eriksson P., Cai L., Radoul M., Chaumeil M.M., Blough M., Luchman H.A., Weiss S., Cairncross J.G., Phillips J.J., Pieper R.O, & Ronen S.M. (2015). IDH1 mutation induces reprogramming of pyruvate metabolism. Cancer research, 75(15), 2999-3009.

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Compound Binding to HSP72-NBD

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To confirm the binding of compounds to HSP72-NBD, a series of CPMG and WaterLOGSY experiments were performed. Compounds were assayed at 200 μM in the presence or absence of 10-μM HSP72-NBD. Two hundred micrometers of ATP were also included in the competition experiments. The total assay volume was 200 μL, and the experiments were performed in 3-mm NMR tubes. The buffer was 25-mM Tris, pH 7.5, 50-mM NaCl, 10% D₂O and 100 μM of DTT in deionized water. NMR experiments were conducted at a ¹H frequency of 600 MHz using a Bruker Avance 600 spectrometer (Bruker, Bilerica, MA, USA) equipped with a 5-mm TCI Cryo-probe. All data were acquired and processed using Topspin (Bruker, Bilerica, MA, USA) and MNova (Mestrelab Research SL, Santiago de Compostela, Spain). The relaxation-edited 1H-NMR spectrum was acquired at 298 K using the CPMG sequence with a spin-lock time of 600 ms. The water signal was suppressed using pre-saturation during the relaxation delay (2 s) and by using the Watergate sequence subsequent to the CPMG sequence. For each spectrum, 64 transients were acquired.

O’Connor S., Le Bihan Y.V., Westwood I.M., Liu M., Mak O.W., Zazeri G., Povinelli A.P., Jones A.M., van Montfort R., Reynisson J, & Collins I. (2022). Discovery and Characterization of a Cryptic Secondary Binding Site in the Molecular Chaperone HSP70. Molecules, 27(3), 817.

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Spectral Analysis of 3-APP Signals in Brain Slices

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Spectral analysis was performed using MNova (Mestrelab Research, Santiago de Compostela, Spain). Each spectrum was zero‐filled to 16,384 points, drift‐corrected, exponentially multiplied with a 10‐Hz line broadening (LB), and baseline corrected. Calculation of the full width at half maximum (FWHM) of the 3‐APP signal in the brain slices was performed using the processed spectra (
FWHMprocessed, with 10‐Hz LB) because the natural FWHM (
FWHMnatural) was difficult to assess due to the high noise level in the non line‐broadened spectra.
The
FWHMnatural of these signals was then derived using Equation (1).

{FWHM}_{natural} = {FWHM}_{processed} - LB .

We note that because 3‐APP accumulation in the brain affected the signal shape and the corresponding linewidth, improvement of signal‐to‐nosie ratio (SNR) by increasing the number of scans would not necessarily provide a better measure of the linewidth.

Shaul D., Grieb B., Lev‐Cohain N., Sosna J., Gomori J.M, & Katz‐Brull R. (2022). Accumulation of 3‐aminopropylphosphonate in the ex vivo brain observed by phosphorus‐31 nuclear magnetic resonance. Nmr in Biomedicine, 35(8), e4721.

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NMR Analysis of Lmod2 EDRR Binding

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The NMR samples were prepared in 20 mM HEPES‐d₁₈ (pH 6.8), which was obtained from the Cambridge Isotope Laboratories (Tewksbury, MA). The samples contained 10% D₂O and 0.2 mM DSS, both purchased from the Cambridge Isotope Laboratories. The concentration of the Lmod2 EDRR was 0.3 mM. The sample was titrated with small aliquots of 10 mM and 30 mM CaCl₂ or MgCl₂ stock solutions (adjusted to pH ~6.8). 1H NMR spectra were recorded at 25°C on a Varian Inova 500 spectrometer (500 MHz) equipped with a 5 mm triple‐resonance probe. The spectra were processed, visualized, and analyzed with Mnova (Mestrelab Research, Santiago de Compostela, Spain).

Smith G.E., Tolkatchev D., Risi C., Little M., Gregorio C.C., Galkin V.E, & Kostyukova A.S. (2022). Ca2+ attenuates nucleation activity of leiomodin. Protein Science : A Publication of the Protein Society, 31(7), e4358.

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Spectral Processing and Intensity Calculation

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Spectral processing was performed using MNova (Mestrelab Research, Santiago de Compostela, Spain). Integrated intensities were calculated either with MNova or with DMFIT^{44 (link)}.

Harris T., Azar A., Sapir G., Gamliel A., Nardi-Schreiber A., Sosna J., Gomori J.M, & Katz-Brull R. (2018). Real-time ex-vivo measurement of brain metabolism using hyperpolarized [1-13C]pyruvate. Scientific Reports, 8, 9564.

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NMR Spectroscopy of Oligosaccharide-Protein Interactions

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Oligosaccharide samples were prepared to a concentration of 1 mm in 10 mm phosphate buffer, pH 7.2, and exchanged by lyophilisation before transfer to a 5 mm NMR tube. Protein was added to a concentration of ∼5 μm, yielding a protein/oligosaccharide ratio of about 1:100. Spectra were recorded at 700 MHz using a Bruker Avance spectrometer equipped with a cryoprobe, at a temperature of either 30 °C or 45 °C. Selective saturation was achieved using a 50 ms adiabatic inversion pulse train irradiating a 950 Hz (1.36 ppm) window at 50 ppm for off-resonance irradiation and typically 7.5 ppm, and -0.3 ppm for protein irradiation. 32 transients of 16K complex points were collected for each irradiation frequency. Processing and subtraction were performed in either Bruker Topspin software or in MNova (Mestrelab Research, Santiago di Compostela, Spain). STD enhancements were calculated as a percentage of the unperturbed spectrum for each individual experiment; where the results of more than one experiment were combined, normalized values were used to improve precision.

Palma A.S., Liu Y., Zhang H., Zhang Y., McCleary B.V., Yu G., Huang Q., Guidolin L.S., Ciocchini A.E., Torosantucci A., Wang D., Carvalho A.L., Fontes C.M., Mulloy B., Childs R.A., Feizi T, & Chai W. (2015). Unravelling Glucan Recognition Systems by Glycome Microarrays Using the Designer Approach and Mass Spectrometry. Molecular & Cellular Proteomics : MCP, 14(4), 974-988.

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SCC-DFTB Modeling of Pyrene-NDI Complexation

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Pyrene–NDI complexation energies were obtained using the self-consistent-charge density functional tight-binding (SCC-DFTB) approach, as implemented within the DFTB+ code.^{42 (link)} Parameters for all atoms and pairs including elements C, H, N, O were taken from the “mio” parameter set of the Slater–Koster library.^{43 (link)} Dispersion corrections based on a Lennard-Jones potential were applied in all simulations.^{44 (link)} Simulations of ¹H NMR spectra were carried out using the “peak table to spectrum” script within Mnova (version 14.1, Mestrelab Research).

Knappert M., Jin T., Midgley S.D., Wu G., Scherman O.A., Grau-Crespo R, & Colquhoun H.M. (2020). Single-site binding of pyrene to poly(ester-imide)s incorporating long spacer-units: prediction of NMR resonance-patterns from a fractal model. Chemical Science, 11(44), 12165-12177.

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Sucrose NMR Spectroscopy Protocol

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Data were collected on a 42mM solution of sucrose in D2O at 25°C on an Agilent 600 MHz Direct Drive spectrometer equipped with a 5 mm cryogenically cooled probe. A standard Agilent pulse program, “NOESY1D”, was used to acquire one-dimensional transient NOE spectra. In this sequence, signals are selected by a pair of Q3 Gaussian cascade pulses flanked by gradients. The particular experiment mimics the generation of a cross peak in a 2D NOE experiment by setting the initial magnetization for the selected pulse to zero. The selective pulse widths varied between 74 and 174 ms depending on the signal being irradiated. A series of mixing times were collected with 512 scans per spectrum to achieve high a signal-to-noise ratio. Data were processed with VNMRJ ( Agilent, Inc.) or with MNova ( Mestrelab Research) software. Typically, data were multiplied by an exponential weighting function that added 1 Hz to the line width, zero filled to 64K points, Fourier transformed, phase corrected and baseline corrected. Peaks were integrated in MNova using manual selection of integral regions.

Chalmers G., Glushka J.N., Foley B.L., Woods R.J, & Prestegard J.H. (2016). Direct NOE Simulation from Long MD Trajectories. Journal of magnetic resonance (San Diego, Calif. : 1997), 265, 1-9.

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MALDI-MS and NMR Spectroscopy Analysis

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MALDI mass spectrometry was conducted using a UltrafleXtreme ABI4700 (Bruker). The samples were dissolved in chloroform at a concentration of 1 mg/mL prior to injection. All NMR spectra were recorded with a 400 MHz Jeol ECS400. Each sample was dissolved in D 2 O and then 1 H and 13 C spectra were collected. The concentration of each sample run was 100 mg/mL. Each spectrum was analysed using MNova (Mestrelab Research) software (v 1.0).

Fussell S.L., King S.M., Royall C.P, & van Duijneveldt J.S. (2022). Oxidative degradation of triblock-copolymer surfactant and its effects on self-assembly. Journal of colloid and interface science, 606(Pt 2).

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