Related Articles

• Need for high resolution 2D spectra

  13C NMR spectra provide wide range chemical shift, and it suggests that can easily distinguish each signals. But carbon resolution of 2D spectra such as HSQC and HMBC is worse than 1D 13C spectra due to small data points. In order to analyze a compound with close 13C chemical shifts, a high resolution 2D spectrum is required frequently. In this document, some improvements to distinguish each signals on 13C axis of 2D hetero nuclear experiments are presented.
• High Mass Resolution MALDI-Imaging MS: High Stability of Peak Position during Imaging MS Measurement

  Matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI-Imaging MS) is a powerful tool for the biochemical analyses of surfaces. Previously, this technique has been used to determine the spatial distribution of hundreds of unknown compounds in thinly sliced tissue sections. The mass spectral images are generated by changing the laser irradiation point at regular intervals across the sample surface and collecting a mass spectrum for each point. Time-of-flight mass spectrometers (TOFMS) are widely used as the mass analyzer for MALDI-Imaging MS because they are well matched for the MALDI ionization process. However, the fine structure of the matrix crystals and small irregularities in the tissue surface flatness can cause peak drift in the collected mass spectra that is caused by slight differences in the starting point of the flight path for the ions at each laser irradiation point. As a result, the typical reflectron type TOFMS systems have a difficult time achieving high mass resolution from spot to spot over a thinly sliced biological surface. Conversely, the JEOL JMS-S3000 “SpiralTOFTM”, which has 5-10 times longer flight path than the reflectron type TOF, is able to reduce the effect of this mass drift to achieve high mass resolution and high mass accuracy. In this work, we report the advantages of using the SpiralTOF for MALDI-Imaging MS analyses of lipids in a mouse brain tissue section.
• High Mass Resolution MALDI-imaging MS Using JMS-S3000 SpiralTOF and msMicroImager

  Imaging mass spectrometry using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-Imaging) has been expanded during the last decade in biological applications, to assess the distribution of proteins, peptides, lipids, drugs, and metabolites in a tissue specimen. In MALDI-Imaging measurements, a laser irradiation point was scanned on a sample surface to acquire a mass spectrum at each point. Analyzing the mass spectra with two-dimensional position information, localization of compounds with inherent molecular weights can be visualized or the mass spectra for certain regions of interests (ROIs) can be created. The JMS-S3000 SpiralTOF (Fig. 1) is a MALDI-TOFMS, which utilizes the JEOL patented spiral ion optical system. It has a 5-10 times longer flight path than the typical reflectron type MALDI-TOFMS. As a result, it can achieve high mass-resolution to separate peaks that have the same nominal mass but have different exact masses (isobaric separation). On the other hand, there are some issues for analyzing high mass resolution and high lateral resolution MALDI-Imaging raw data with common imaging software options such as Biomap.
• High Resolution and High Mass Accuracy MALDI-ISD Measurements

  Matrix assisted laser desorption/ionization (MALDI) combined with in-source decay (ISD) is a useful tool for doing top-down sequencing of intact proteins. This technique can provide enough information to determine both N- and C-terminal sequences. In this work, we measured the ISD fragment ions generated for several peptides using the JEOL SpiralTOF MALDI-MS system.
• The occupied/emptied sites analysis of Lithium Titanium Oxide anodes: How can we obtain high resolution solid state Lithium NMR spectra? _NM200001E

  Lithium ion secondary batteries using spinel-type lithium titanium oxide (LTO) as the negative electrode material are excellent in safety and cycle characteristics due to their chemical stability, and have already been put into practical use.
• Experimental set-up of high-resolution 1H solid-state NMR by wPMLG_NM200010E

  1H, in principle, is very useful nucleus to investigate atomic-resolution structures and dynamics due to its high abundance (>99%) and gyromagnetic ratio (600 MHz at 14.1T). In fact 1H is the first choice of nucleus in solution NMR. On the other hand, 1H NMR of rigid solids is much less common. This is because 1H solid-state NMR gives very broad (~50 kHz) and featureless spectra (Fig 1a) due to strong 1H-1H dipolar coupling, which is dynamically averaged out in solution. Magic angle spinning (MAS) removes the broadening to the first order, but is not enough to achieve high resolution 1H NMR at moderate MAS rate (Fig 1b). Tremendous efforts were made to overcome this issue from the early dates of solid-state NMR towards high-resolution 1H NMR [1]. Most of them combine MAS with sophisticated 1H pulses which is dubbed CRAMPS (combined rotation and multiple pulse spectroscopy). Nowadays very fast MAS > 60 kHz can be used to achieve high-resolution 1H solid-state NMR (Fig 1c) [2]. However, the traditional CRAMPS is still useful as that can be performed with very conventional solid-state NMR equipment, for example 4 mm MAS probe with a 400 MHz spectrometer. Moreover, wPMLG at moderate MAS rate often overwhelms fast MAS in terms of resolution. In this note, we will describe tutorial guidance to optimize experimental parameters for CRAMPS.