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Signal-to-noise of a chromatographic peak from a single measurement has been used determine the performance of two different MS systems, but this parameter can no longer be universally applied and often fails to provide meaningful estimates of the instrument detection limits (IDL).

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Mass spectrometers are effective for identifying and quantifying unknown molecules, such as disease-related proteins and small molecules in pharmaceutical research and medical diagnosis. In addition, mass spectrometry (MS) can be particularly powerful when analyzing molecules with complex structures, such as posttranslationally modified proteins. Among various MS approaches, high-resolution multistep tandem MS (MS-MS) is an emerging methodology for accurate identification of complex molecules. In this article, we describe a new approach for mass analysis with enhanced quantitative capability combined with high-resolution multistep MS-MS, where the dynamic range of quantitation covers four orders of magnitude.

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Horiba Jobin Yvon, Inc.

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Chromium is a key ingredient in a number of metal alloys used for metal implants which, despite being coated with inert surface layer coatings, can break down over time as a result of biocorrosion. Leeching of metal ions from implants into surrounding bone, tissue, and body fluids can cause severe health problems. Although the toxicity of the metal is low, there is a potential health risk if chromium ions enter the body. In ICP-MS, the chromium (52Cr) signal can be affected by interference from the recombination of background plasma 40Ar and sample-specific matrix 12C. To eliminate this interference, hydrogen can be used in the iCRC as a reaction gas to allow accurate analysis of 52Cr. Results using certified clinical standards of chromium in blood, plasma, urine, and serum clearly demonstrate the benefit of using hydrogen as a collision gas to remove the argon-carbide polyatomic interference. This study shows that ICP-MS is an essential tool for clinical monitoring of metal ions in complex matrices and that hydrogen iCRC gas allowed for greater accuracy and a lower level of quantitation in clinical matrices.

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Mass spectrometers are effective for identifying and quantifying unknown molecules, such as disease-related proteins and small molecules in pharmaceutical research and medical diagnosis. In addition, mass spectrometry (MS) can be particularly powerful when analyzing molecules with complex structures, such as posttranslationally modified proteins. Among various MS approaches, high-resolution multistep tandem MS (MS-MS) is an emerging methodology for accurate identification of complex molecules. In this article, we describe a new approach for mass analysis with enhanced quantitative capability combined with high-resolution multistep MS-MS, where the dynamic range of quantitation covers four orders of magnitude.

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In Parts I-III of this series, columnist David W. Ball recounted the failings of classical mechanics, the quantum hypothesis, and the rise of a new theory called quantum mechanics. In this installment, he discusses the ideal systems whose wavefunctions can be determined exactly from the Schr?dinger equation.

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PIKE Technologies, Inc.

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A common endpoint for a biomarker discovery experiment is a list of putative marker proteins. The next step is then to perform targeted quantitative measurements of these proteins in an expanded patient population to assess their validity as markers. Analytical accuracy and precision are required for unambiguous quantitative analysis of targeted proteins from very complex mixtures. Wide dynamic range and high sensitivity are critical for detecting low-abundance proteins. Such an assay also is appropriate for "targeted discovery" experiments, where the goal is to quantitate a large number (up to hundreds) of known proteins in a complex sample.

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In ATR/FT-IR, magnified visual monitoring of a sample benefits many applications. For micro-sampling and defect analysis, viewing capabilities decrease overall measurement time by allowing the user to locate the desired sampling area quickly and enhance confidence in the collected data by assuring the sampling point. Visual changes in the sample also may be easily monitored during testing. As an example application, the ease of micro-sampling is shown through fiber analysis and the results are discussed.

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Here we describe a new compact device for electron-capture dissociation (ECD) analysis of large peptides and posttranslational modifications of proteins, which can be difficult to analyze via conventional dissociation techniques such as collision-induced dissociation (CID). The new compact device realizes ECD in a radio frequency (RF) linear ion trap equipped with a small permanent magnet, which is significantly different than the large and maintenance-intensive superconducting magnet required for conventional ECD in Fourier-transform ion cyclotron resonance mass spectrometers. In addition to its compactness and ease of operation, an additional merit of an RF linear ion trap ECD is that its reaction speed is fast, comparable to CID, enabling data acquisition on the liquid-chromatography (LC) time scale. We interfaced the linear-trap ECD device to a time-of-flight mass spectrometer to obtain ECD spectra of phosphorylated peptides injected into a liquid chromatograph, infused glycopeptides, and intact small..

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This article introduces the application of high-resolution ultrasonic spectroscopy for the analysis of emulsions and suspensions.

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Seeking opportunities for career growth is important for early-career scientists to explore new skills, connect with mentors, and gain insights into the field. Professional societies and educational programs can be invaluable resources, providing mentorship, training, and networking opportunities that can accelerate career success in spectroscopy.

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This article describes the use of Raman microscopy to investigate historical mysteries in rock art and frescoes.

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The authors show that high resolution 1H nuclear magnetic resonance (NMR) spectroscopy can be used to study biofilm metabolism under environmentally relevant conditions in a minimally invasive way.

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Lambda Solutions, Inc.

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The structural complexity of monoclonal antibodies (mAbs) challenges the capabilities of even the most advanced chromatography and mass spectrometry techniques. This study examines the use of micro-pillar array columns in combination with mass spectrometry for peptide mapping of both mAbs and antibody–drug conjugates (ADCs).

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This issue contains interviews that provide an excellent sampling of the fascinating science that will be presented at this year’s SciX conference.

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The study of the interaction mechanism of nucleic acids-CTMAB with AG showed that the enhanced RLS comes from the aggregation of AG on nucleic acids through the bridged and synergistic effect of CTMAB.

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Serum protein profiling using mass spectrometry (MS) is one of the most promising approaches for biomarker identification. The authors adopted a nano liquid chromatography (nLC)–linear ion trap time-of-flight (LIT-TOF) MS system and newly developed software known as information-based acquisition (IBA) to identify biomarkers in human serum. IBA is a data processing protocol for repetitive MS analyses. Peptides selected for the first-pass MS-MS analysis are automatically excluded from the MS spectrum such that subsequent MS-MS analyses are performed on different peptides to minimize overlapping analyses, resulting in the identification of relatively low-abundant peptides.

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Here we describe a new compact device for electron-capture dissociation (ECD) analysis of large peptides and posttranslational modifications of proteins, which can be difficult to analyze via conventional dissociation techniques such as collision-induced dissociation (CID). The new compact device realizes ECD in a radio frequency (RF) linear ion trap equipped with a small permanent magnet, which is significantly different than the large and maintenance-intensive superconducting magnet required for conventional ECD in Fourier-transform ion cyclotron resonance mass spectrometers. In addition to its compactness and ease of operation, an additional merit of an RF linear ion trap ECD is that its reaction speed is fast, comparable to CID, enabling data acquisition on the liquid-chromatography (LC) time scale. We interfaced the linear-trap ECD device to a time-of-flight mass spectrometer to obtain ECD spectra of phosphorylated peptides injected into a liquid chromatograph, infused glycopeptides, and intact small..

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It makes intuitive sense - the higher the sensitivity of an inductively coupled plasma–mass spectrometry (ICP-MS) system, the lower the detection limit. But there are many factors that affect the detection limit for a given isotope in a given sample. These factors include sensitivity, background noise, and interferences.

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The authors show that high resolution 1H nuclear magnetic resonance (NMR) spectroscopy can be used to study biofilm metabolism under environmentally relevant conditions in a minimally invasive way.

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It makes intuitive sense - the higher the sensitivity of an inductively coupled plasma–mass spectrometry (ICP-MS) system, the lower the detection limit. But there are many factors that affect the detection limit for a given isotope in a given sample. These factors include sensitivity, background noise, and interferences.

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Lambda Solutions, Inc.

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SPEX CertiPrep, Inc.

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Mass spectrometry plays an increasingly significant role in the analysis of residues and contaminants in food. Here we will illustrate how the combination of ultrahigh-pressure liquid chromatography (UHPLC) and high-resolution time-of-flight-mass spectrometry (TOF-MS) is used to generate a screen of veterinary drug residues in products of animal origin. The use of UHPLC–TOF-MS and dedicated, workflow directed software allows rapid screening for large numbers of residues and automated quantification of positive samples. In addition, we illustrate how the data generated using MSE acquisition mode enable critical structural information to be collected, which offers additional selectivity and confirmatory data for compound identification and facilitates elucidation of the structure of newly discovered compounds.

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Thermo Fisher Scientific