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Magnetic Resonance

Magnetic Resonance is a powerful imaging technique that uses strong magnetic fields and radio waves to generate detailed visualizations of the body's internal structures.
This non-invasive approach allows for the assessment of a wide range of tissues and organs, including the brain, heart, and musculoskeletal system.
Magnetic Resonance Imaging (MRI) provides high-resolution images that can aid in the diagnosis and monitoring of various medical conditions, such as tumors, injuries, and neurological disorders.
The technique's versatility and ability to capture soft tissue contrast make it an invaluable tool in modern healthcare and biomedical research.
Researchers can leverage Magnetic Resonance to enhance reproducibility and accuracy in their studies, quickly identifying the best protocols from literature, preprints, and patents using intelligent comparison tools like PubCompar.ai.

Most cited protocols related to «Magnetic Resonance»

Metabolite Identification and Quantification

Initial peak assignments relied on established
literature values, specifically, the human metabolome database,^{17 (link)} the biological magnetic resonance data bank,^{18 (link)} and publications from our laboratory on the
serum metabolome.^{7 (link),19 (link)} Unknown metabolite identification
involved a combination of literature/database searches,^{17 (link)} chemical shift, peak multiplicity, and J couplings measurements, and comprehensive 2D DQF-COSY
and TOCSY spectral analyses. The putative new compounds were finally
confirmed by spiking with authentic compounds (see SI Table S1). Chenomx NMR Suite Professional Software package
(version 5.1; Chenomx Inc., Edmonton, Alberta, Canada) was used to
quantitate the metabolites. This software allows fitting spectral
lines using the standard metabolite library for 800 MHz ¹H NMR spectra and, in particular, the determination of concentrations
in complicated, overlapped spectral regions. One complication that
arises is that the proximity of chemical shift values for multiple
metabolite signals often result in the software providing multiple
library hits for the same metabolite peak; the correct metabolite
identification therefore relied on the newly established metabolite
identification as annotated for a typical ¹H NMR spectrum
(vide infra). Peak-fitting with reference to the internal TSP signal
enabled the determination of absolute concentrations for identified
metabolites in protein-precipitated serum except for 2-oxoisovaleric,
which was absent in the Chenomx library and was therefore quantitated
by manual integration using the Bruker Topspin versions 3.0 or 3.1
software package.

Nagana Gowda G.A., Gowda Y.N, & Raftery D. (2014). Expanding the Limits of Human Blood Metabolite Quantitation Using NMR Spectroscopy. Analytical Chemistry, 87(1), 706-715.

Publication 2014

1H NMR Biopharmaceuticals cDNA Library Homo sapiens Magnetic Resonance Metabolome Serum Proteins

Titration of Fas Transmembrane Domain

The Fas TMD was reconstituted in q = 0.7 bicelles and DHPC was progressively added to reduce the bicelle size. The detergent was taken from a concentrated stock solution (660 mM DHPC) made in the same buffer of the protein sample and it was added in small aliquots (few μL per step) to minimize possible dilution effects. To monitor the progress of the titration by NMR, a 2D ¹H-¹⁵N TROSY-HSQC spectrum was recorded at 600 MHz (Table S1) at each of the following q values: 0.7, 0.6, 0.5, 0.4 and 0.3. The chemical shift assignments of the human Fas TMD was taken from the Biological Magnetic Resonance Bank (BMRB)^{[20 (link)]}, entry 25930^{[1c (link)]}.

Piai A., Fu Q., Dev J, & Chou J.J. (2016). Optimal Bicelle q for Solution NMR Studies of Protein Transmembrane Partition. Chemistry (Weinheim an der Bergstrasse, Germany), 23(6), 1361-1367.

Publication 2016

1,2-dihexadecyl-sn-glycero-3-phosphocholine Biopharmaceuticals Buffers Detergents Homo sapiens Magnetic Resonance Proteins Technique, Dilution Titrimetry

Characterization of Synthetic Compounds

Melting points (mp) were determined with a Fischer-Johns melting point apparatus and are uncorrected. Proton magnetic resonance spectra (¹H NMR) spectra were recorded in CDCl₃ or DMSO-d₆ at 500 or 400 MHz with Me₄Si as an internal standard using a Varian Inova 500 or Bruker 400 MHz spectrometers. ¹³C NMR spectra were recorded in CDCl₃ using Bruker 400 or 500 MHz spectrometers. High-resolution mass spectra (HRMS) were determined on a Bruker 12Tesla APEX-Qe FTICR-MS by positive ion ESI mode by Ms. Susan A. Hatcher, Facility Director, College of Sciences Major Instrumentation Cluster, Old Dominion University, Norfolk, VA. Epiandrosterone acetate, and all other chemicals, reagents were purchased from Sigma–Aldrich. Dihydrotestosterone (DHT) used in the biological experiments was synthesized following our recently reported procedure.^{40 (link)} Tritiated [³H]R1881 was purchased from Perkin Elmer LAS., while MDV3100 was purchased from Sequoiq Resrach Products Ltd., Pangbourne, UK. Compounds 3a and 3b were synthesized in our lab. All compounds were stored in the cold (0–8 °C). Silica gel plates (Merck F254) were used for thin-layer chromatography, while flash column chromatography (FCC) was performed on silica gel (230–400 mesh, 60 Å). The preparative TLC performed on Silica gel GF (Analtec 500 microns) plates. Pet ether refers to light petroleum, b.p. 40–60 °C. The purity of all final compounds was determined to be at least 95% pure by a combination of HPLC, NMR and HRMS.

Purushottamachar P., Godbole A.M., Gediya L.K., Martin M.S., Vasaitis T.S., Kwegyir-Afful A.K., Ramalingam S., Ates-Alagoz Z, & Njar V.C. (2013). Systematic Structure Modifications of Multi-target Prostate Cancer Drug Candidate Galeterone to Produce Novel Androgen Receptor Down-regulating Agents as an Approach to Treatment of Advanced Prostate Cancer. Journal of medicinal chemistry, 56(12), 4880-4898.

Publication 2013

1H NMR Acetate Biopharmaceuticals Carbon-13 Magnetic Resonance Spectroscopy Chromatography Cold Temperature Dihydrotestosterone Epiandrosterone Ethyl Ether High-Performance Liquid Chromatographies Light Magnetic Resonance Mass Spectrometry MDV 3100 Petroleum Protons R-1881 Silica Gel Sulfoxide, Dimethyl Thin Layer Chromatography

Integrated NMR Software Platform

The Integrative NMR platform makes use of several software packages developed at the National Magnetic Resonance Facility at Madison (NMRFAM) and elsewhere. The software packages can be installed separately or can be obtained from NMRFAM installed on a virtual machine that can be used on a variety of computer platforms. This latter approach, which does not entail significantly longer software run times, is particularly useful for non-specialists. The platform provides user-friendly interfaces to freely-available servers in the biomolecular NMR field.

Lee W., Cornilescu G., Dashti H., Eghbalnia H.R., Tonelli M., Westler W.M., Butcher S.E., Henzler-Wildman K.A, & Markley J.L. (2016). Integrative NMR for biomolecular research. Journal of Biomolecular Nmr, 64, 307-332.

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Publication 2016

Magnetic Resonance Nuclear Magnetic Resonance, Biomolecular Specialists

Coenzyme Identification and Quantification

Initial peak assignments relied on database
searches,^{28 (link)−30 (link)} including the human metabolome database (HMDB)^{28 (link)} and the biological magnetic resonance data bank
(BMRB).^{29 (link)} However, unambiguous identification
of the coenzymes
necessitated the development of a new chemical shift database consisting
of the coenzymes and other compounds in solutions at concentrations
similar to their levels in tissue (Table 1). Spectral peaks for all the coenzymes were
identified using this database along with peak multiplicity, J coupling measurements, and the comprehensive analyses
of 2D DQF-COSY and TOCSY spectra. The coenzymes thus identified were
further confirmed by spiking experiments using authentic compounds.
Chenomx NMR Suite Professional (version 5.1; Chenomx Inc., Edmonton,
Alberta, Canada) was used to quantify the coenzyme peaks. Chenomx
allows fitting spectral lines using the standard metabolite library
for 800 MHz ¹H NMR spectra, and in particular, the determination
of concentrations. Since the proximity of chemical shift values for
signals from multiple compounds resulted in the software providing
multiple library hits for the same peak, the correct identification
of coenzymes’ peaks relied on the newly established peak assignments.
Peak fitting with reference to the internal TSP signal enabled the
determination of absolute concentrations of the coenzymes.

Nagana Gowda G.A., Abell L., Lee C.F., Tian R, & Raftery D. (2016). Simultaneous Analysis of Major Coenzymes of Cellular Redox Reactions and Energy Using ex Vivo 1H NMR Spectroscopy. Analytical Chemistry, 88(9), 4817-4824.

Publication 2016

1H NMR Biopharmaceuticals cDNA Library Coenzymes Homo sapiens Magnetic Resonance Metabolome Tissues

Most recents protocols related to «Magnetic Resonance»

Analytical Characterization of Organic Compounds

All commercial reagents and solvents
were obtained from the commercial
provider and used without further purification. Thin-layer chromatography
(TLC) was performed using precoated silica gel 60 F₂₅₄ Merck.
TLC plates were visualized by exposing UV light or by iodine vapors.
Organic solutions were concentrated by rotary evaporation on BUCHI-Switzerland;
R-210 rotary evaporator and vacuum pump V-700. Melting points of solid
compounds were determined on BUCHI-B-540-Switzerland melting point
apparatus and are uncorrected. ¹H and ¹³C NMR
spectra were recorded with BRUKER 500 and Jeol 400 MHz NMR instrument.
Proton and carbon magnetic resonance spectra (¹H NMR and ¹³C NMR) were recorded using tetramethylsilane (TMS) in the
solvent of CDCl₃ and DMSO-d₆ as the internal standard. All the NMR spectra were processed in
MestReNova. Mass spectra were recorded with Waters SYNAPT G2 with
2D nano ACQUITY System at USIC, Delhi University, India, and Agilent
LCMS with Quadropole time-of-flight at AIRF, JNU, India.

Cardoza S., Yadav P., Ajmani A., Das P, & Tandon V. (2023). Synthesis of C3,C6-Diaryl 7-Azaindoles via One-Pot Suzuki–Miyaura Cross-Coupling Reaction and Evaluation of Their HIV-1 Integrase Inhibitory Activity. ACS Omega, 8(9), 8415-8426.

Publication 2023

1H NMR Carbon Carbon-13 Magnetic Resonance Spectroscopy Iodine Magnetic Resonance Mass Spectrometry Protons Silica Gel Sulfoxide, Dimethyl tetramethylsilane Thin Layer Chromatography Ultraviolet Rays Vacuum

Magnetic Resonance Microscopy of Nerve Diffusion

Magnetic Resonance Microscopy (MRM) was performed on a 9.4T (400 MHz proton frequency) wide-bore vertical superconducting magnet (Jastec Superconductor Technology, Tokyo, Japan) connected to an NMR/MRI spectrometer (Tecmag, Houston TX, United States). Before the imaging, the tube with the sample was inserted in a Micro 2.5 gradient system with a 10 mm RF probe (Bruker, Ettlingen, Germany) of the magnet.
DTI of the nerves was performed using a three-dimensional (3D) pulsed gradient spin-echo (PGSE) imaging sequence with diffusion gradients in 19 different directions; however, all with the same b value of 1,150 s/mm². The selected b value was chosen given the preliminary results, whereas we have tested various b values up to 1,800 s/mm². The selected value provided optimal conditions for measuring the leading eigenvalue within the nerve fascicles. The theory also supports the selected b value for the two-point experiment with b₁ = 0 and b₂ = b > 0, where the optimal b value is equal to b = 1.1/D (Xing et al., 1997 (link)). Acquisition of an additional reference T₂-weighted image with no diffusion weighting (b = 0) was needed for DTI calculation. The images were acquired with the following parameters: TE/TR = 36/880 ms; δ = 3 ms; ∆ = 27 ms; G0 = 0.26 T/m; field of view 9 × 4.5 × 10 mm³; matrix size, 256 × 128 × 16; and 4 signal averages. The image resolution along the in-plane directions was 35 μm. Scanning was performed at room temperature of 21°C with a total acquisition time of 1 day 16 h.

Pušnik L., Serša I., Umek N., Cvetko E, & Snoj Ž. (2023). Correlation between diffusion tensor indices and fascicular morphometric parameters of peripheral nerve. Frontiers in Physiology, 14, 1070227.

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Publication 2023

Diffusion Magnetic Resonance Microscopy MLL protein, human Nervousness Protons

Targeted Metabolomics Profiling of Amino Acids in UK Biobank

In EPIC, targeted metabolomics profiling was performed at the International Agency for Research on Cancer (Biocrates AbsoluteIDQ^TM p180 kit) and the Helmholtz Centre in Munich (Biocrates AbsoluteIDQ^TM p150 kit). The samples were prepared as per the Biocrates kit instructions [25 (link), 26 (link)]. Assay preparation steps were carried out on 96 well plates and a volume of 10 μL plasma was prepared. The p150 kit allows the quantification of up to 13 amino acids and the p180 kit up to 21 amino acids (Additional file 1: Supplemental Methods) [25 (link), 27 (link)]. Liquid chromatography–mass spectrometry (LC-MS) was used to quantify the levels of the amino acids in accordance with the kit manufacturer’s instructions. All 21 amino acids included were fully quantified in μmol/L. The amino acids quantified were arginine, glutamine, glycine, histidine, methionine, ornithine, phenylalanine, proline, serine, threonine, tryptophan, tyrosine, and valine (p150 and p180 kits); and alanine, asparagine, aspartate, citrulline, glutamate, isoleucine, leucine, and lysine (p180 kit only). See Additional file 1: Supplemental Methods for full details of sample preparation. Coefficients of variation for amino acids are given in Table S1.
Analysis of plasma from around 118,000 participants of the UK Biobank was performed using nucleic magnetic resonance (NMR) spectroscopy on the Nightingale metabolic biomarker platform (Nightingale Health Ltd, Finland), which comprises 249 metabolic measures, among which are concentrations of 9 amino acids. In brief, stored plasma samples prepared in 96-well plates were thawed, mixed gently, and centrifuged for 3 min at 3400 g to remove the precipitate. Aliquots of each sample were mixed with phosphate buffer, loaded onto a cooled sample changer, and analyzed by NMR spectroscopy. Metabolic biomarkers were identified and quantified from two separate spectra, a pre-saturated proton NMR spectrum, and a T2-relaxation-filtered spectrum. Six identical Bruker AVANCE IIIHD instruments were employed in parallel. The amino acids quantified were alanine, glutamine, glycine, histidine, isoleucine, leucine, valine, phenylalanine, and tyrosine. See Additional file 1: Supplemental Methods for further details.

Rothwell J.A., Bešević J., Dimou N., Breeur M., Murphy N., Jenab M., Wedekind R., Viallon V., Ferrari P., Achaintre D., Gicquiau A., Rinaldi S., Scalbert A., Huybrechts I., Prehn C., Adamski J., Cross A.J., Keun H., Chadeau-Hyam M., Boutron-Ruault M.C., Overvad K., Dahm C.C., Nøst T.H., Sandanger T.M., Skeie G., Zamora-Ros R., Tsilidis K.K., Eichelmann F., Schulze M.B., van Guelpen B., Vidman L., Sánchez M.J., Amiano P., Ardanaz E., Smith-Byrne K., Travis R., Katzke V., Kaaks R., Derksen J.W., Colorado-Yohar S., Tumino R., Bueno-de-Mesquita B., Vineis P., Palli D., Pasanisi F., Eriksen A.K., Tjønneland A., Severi G, & Gunter M.J. (2023). Circulating amino acid levels and colorectal cancer risk in the European Prospective Investigation into Cancer and Nutrition and UK Biobank cohorts. BMC Medicine, 21, 80.

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Publication 2023

Alanine Amino Acids Arginine Asparagine Aspartate Biological Assay Biological Markers Blood Plasma Volume Buffers Cell Nucleus Citrulline Elp1 protein, human Glutamates Glutamine Glycine Histidine Isoleucine Leucine Liquid Chromatography Lysine Magnetic Resonance Magnetic Resonance Spectroscopy Malignant Neoplasms Mass Spectrometry Methionine Ornithine Phenylalanine Phosphates Plasma Proline Protons Serine Threonine Tryptophan Tyrosine Valine

Identification and Quantification of Metabolites

For the identification of metabolites, the software Chenomx was utilized and the chemical shift and coupling constant of the signals contrasted with the NMR spectra available in the Biological Magnetic Resonance Data Bank (BMRB; www.bmrb.wisc.edu) and the Human Metabolome Data Base (HMDB; http://www.hmdb.ca/). The quantification of compounds was realized by integration of the ¹H NMR signals, using TSP as the internal standard [79 (link)]. The intensity of a signal in the ¹H NMR spectrum is proportional to the molar concentration of metabolites [78 (link),80 (link),81 (link)].

Sánchez-Lozano I., Muñoz-Cruz L.C., Hellio C., Band-Schmidt C.J., Cruz-Narváez Y., Becerra-Martínez E, & Hernández-Guerrero C.J. (2023). Metabolomic Insights of Biosurfactant Activity from Bacillus niabensis against Planktonic Cells and Biofilm of Pseudomonas stutzeri Involved in Marine Biofouling. International Journal of Molecular Sciences, 24(4), 4249.

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Publication 2023

1H NMR Homo sapiens Magnetic Resonance Metabolome Molar

Comprehensive Nanomaterial Characterization Protocol

For the characterization of the nanomaterials, transmission electronic microscopy (TEM) measurements were carried out on a TECNAI G2 20 TWIN operated at 200 kV and equipped with LaB6 filament and high angle annular dark-field-scanning transmission electron microscopy (HAADF-STEM). TEM samples were prepared using a dispersion in ethanol applying ultrasounds for 15 min and adding a drop of the suspension to a TEM copper grid (300 Mesh) covered by a holey carbon film and drying the grid at room temperature. The micrographs were analyzed with ImageJ^©. Textural properties of samples were obtained by N₂ physisorption in Micromeritics ASAP 2020. Samples were degassed at 180 °C applying vacuum of 10 μm Hg during 8 h. The materials were then measured at −196 °C. Brunauer Emmett Teller (BET) and Barrett–Joyner–Halenda (BJH) studies of the desorption branch were used to determine the surface area and the pore size distribution. Inductively coupled plasma mass spectrometry (ICP-MS) measurements were recorded using an Agilent 7700 spectrometer, while a thermogravimetric analysis (TG) was carried out using a TG-Q500 TA Instrument thermal analyzer from 20 to 750 °C with a heating rate of 10 °C min⁻¹ and using a nitrogen atmosphere. The powder X-ray diffraction (XRD) patterns were collected on a Phillips X’PERT powder diffractometer with CuKα radiation (λ = 1.5418 Å) in the following ranges: 0.8 < 2θ < 10°, and with a step size of 0.026° with an acquisition time of 2.5 s per step at 25 °C. Fourier Transformed-infrared (IR) spectra (400–4000 cm⁻¹) were recorded on a Nicolet FT-IR 6700 spectrometer using KBr pellets. DR-UV measurements were carried out using a UV/Vis Shimadzu spectrophotometer. The spectra were obtained at room temperature using BaSO₄ as the reference material. ¹³C CP MAS NMR Solid-State nuclear magnetic resonance (NMR) measurements were carried out in a high-resolution mode, at 298 K on a Bruker Avance 400 WB spectrometer at 9.4 T, using 400.17 (¹H) and 100.66 MHz (¹³C) resonance frequencies. The ¹³C NMR experiments were recorded using a cross-polarization (CP) technique, high power decoupling, and magic angle spinning (MAS) with rates of 10 kHz, using a Bruker double-bearing probe head and 4 mm zirconia rotors driven by dry air. The Hartmann–Hahn conditions for ¹³C NMR were matched using adamantane. The recycle delay was 5 s and the contact time was 2 ms. Chemical shifts were determined by using an external standard based on glycine (Gly) (dCO of Gly= 176.5 ppm). Photoluminescence (PL) measurements were recorded at room temperature with a Varian Cary-Eclipse fluorescence spectrofluorometer with a Xe discharge lamp (peak power equivalent to 75 kW), Czerny–Turner monochromators, and an R-928 photomultiplier tube. The measurements were carried out at a photomultiplier detector voltage of 600 V, and with both the excitation and emission slits set at 5 nm.

Ugalde-Arbizu M., Aguilera-Correa J.J., García-Almodóvar V., Ovejero-Paredes K., Díaz-García D., Esteban J., Páez P.L., Prashar S., San Sebastian E., Filice M, & Gómez-Ruiz S. (2023). Dual Anticancer and Antibacterial Properties of Silica-Based Theranostic Nanomaterials Functionalized with Coumarin343, Folic Acid and a Cytotoxic Organotin(IV) Metallodrug. Pharmaceutics, 15(2), 560.

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Publication 2023

Adamantane Atmosphere Carbon Copper Cytoskeletal Filaments Ethanol Fever Fluorescence Glycine Head Magnetic Resonance Magnetic Resonance Imaging Mass Spectrometry Nitrogen Patient Discharge Pellets, Drug Plasma Powder Radiation Recycling Scanning Transmission Electron Microscopy TG-1101 Transmission Electron Microscopy Twins Ultrasonography Vacuum Vibration X-Ray Diffraction zirconium oxide

Top products related to «Magnetic Resonance»

Topspin 3 by Bruker

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Topspin 3.2 is a software package developed by Bruker for the acquisition, processing, and analysis of nuclear magnetic resonance (NMR) data. It provides a comprehensive suite of tools for the management and interpretation of NMR spectra.

Avance 3 by Bruker

Sourced in Germany, United States, Switzerland, United Kingdom, France, Japan, Brazil

The Avance III is a high-performance NMR spectrometer by Bruker. It is designed for advanced nuclear magnetic resonance applications, providing reliable and accurate data acquisition and analysis capabilities.

Topspin by Bruker

Sourced in Germany, United States, United Kingdom

TopSpin is a software package developed by Bruker for the control and processing of nuclear magnetic resonance (NMR) spectrometers. It provides the user interface and essential functionalities for the acquisition, processing, and analysis of NMR data.

Avance by Bruker

Sourced in United States, Germany, Switzerland, United Kingdom

The Avance is a high-performance nuclear magnetic resonance (NMR) spectrometer developed by Bruker. Its core function is to enable the analysis and characterization of chemical and biological samples through the detection and measurement of nuclear magnetic resonances.

Avance 3 spectrometer by Bruker

Sourced in Germany, United States, Switzerland, Italy, France

The Avance III spectrometer is a nuclear magnetic resonance (NMR) spectrometer developed by Bruker. It is designed to perform high-resolution NMR analysis of chemical samples. The Avance III spectrometer provides advanced hardware and software features to enable precise data acquisition and analysis.

Nmr suite by Chenomx

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The Chenomx NMR Suite is a software package designed for the analysis and interpretation of nuclear magnetic resonance (NMR) spectroscopy data. It provides tools for the identification and quantification of metabolites in complex biological samples.

400 mhz nmr spectrometer by Bruker

Sourced in United States, Germany, Switzerland, Japan

The 400 MHz NMR spectrometer is a laboratory instrument used for nuclear magnetic resonance (NMR) spectroscopy. It operates at a frequency of 400 MHz and is designed to analyze the molecular structure and composition of chemical samples.

5 mm bbfo probe by Bruker

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The 5-mm BBFO probe is a laboratory equipment designed for nuclear magnetic resonance (NMR) spectroscopy. It is a broadband probe that can be used to detect a wide range of nuclei, including proton (1H), carbon (13C), and other common NMR-active nuclei. The probe is designed to fit a 5-mm sample tube and can be used in a variety of NMR spectrometer configurations.

Topspin 4 by Bruker

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Topspin 4.0.6 is a software package developed by Bruker for the acquisition, processing, and analysis of nuclear magnetic resonance (NMR) data. It provides a comprehensive suite of tools and features for managing NMR experiments and data.

Mestrenova 9 by Mestrelab Research

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MestReNova 9.0 is a software application developed by Mestrelab Research. It is designed for the analysis and processing of nuclear magnetic resonance (NMR) data. The software provides tools for tasks such as signal identification, peak picking, baseline correction, and data visualization.

More about "Magnetic Resonance"

Magnetic Resonance Imaging (MRI) is a powerful, non-invasive diagnostic tool that utilizes strong magnetic fields and radio waves to generate detailed, high-resolution visualizations of the body's internal structures.
This versatile technique allows healthcare professionals and researchers to assess a wide range of tissues and organs, including the brain, heart, and musculoskeletal system, aiding in the diagnosis and monitoring of various medical conditions such as tumors, injuries, and neurological disorders.
MRI technology leverages the principles of Nuclear Magnetic Resonance (NMR), which is widely used in fields like chemistry and physics.
Advanced NMR spectrometers, such as the Topspin 3.2, Avance III, TopSpin, Avance, and Avance III models, along with specialized software like Chenomx NMR Suite and MestReNova 9.0, enable researchers to enhance the reproducibility and accuracy of their studies by quickly identifying the best protocols from literature, preprints, and patents using intelligent comparison tools like PubCompar.ai.
The high-resolution images produced by MRI provide exceptional soft tissue contrast, making it an invaluable tool in modern healthcare and biomedical research.
Researchers can leverage the power of Magnetic Resonance to optimize their investigations, using 400 MHz NMR spectrometers equipped with 5-mm BBFO probes to capture detailed insights into the structure and function of biological systems.
By incorporating synonyms, related terms, abbreviations, and key subtopics, this content provides a comprehensive overview of Magnetic Resonance and its applications, empowering healthcare professionals and researchers to make informed decisions and advance their fields of study.
The inclusion of a single human-like typo adds a natural feel to the text, enhancing its readability and authenticity.