GC-MS with Cold EI improves all of the central GC-MS performance aspects, but it is known mostly for its provision of enhanced molecular ions. This occasionally leads to the misconception that, like chemical ionization, Cold EI is a supplementary ion source to standard EI. However, Cold EI is a highly superior replacement ion source to standard EI. While Cold EI mass spectra are the most informative and fully compatible with mass spectral library (such as NIST) identification, in some cases, the Cold EI mass spectra with their enhanced molecular ions result in a "picture" that is not as one is used to seeing. In this paper, we describe the "Cool Classical EI" mode, which produces classical EI mass spectra like standard EI. The change of Cold EI into the Cool Classical EI mode is software-based, requires no hardware change, and can be achieved even during the analysis. Several mass spectra that were obtained in the Cool Classical EI mode are presented and compared with standard EI and Cold EI mass spectra. In this paper we further demonstrate and discuss several benefits that Cold EI brings that are retained while using Cool Classical EI, including (a) much faster speed of analysis, (b) uniform response, (c) extended range of compounds amenable for analysis, (d) improved sample identification, (e) elimination of ion source related peak tailing, (f) elimination of intraion-source degradation, and (g) better signal-to-noise ratio of the sample compounds.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11311530 | PMC |
http://dx.doi.org/10.1021/jasms.4c00265 | DOI Listing |
J Proteome Res
January 2025
Department of Chemistry, University of Texas at Austin, Austin, Texas 78712, United States.
Proteo-SAFARI is a shiny application for fragment assignment by relative isotopes, an R-based software application designed for identification of protein fragment ions directly in the / domain. This program provides an open-source, user-friendly application for identification of fragment ions from a candidate protein sequence with support for custom covalent modifications and various visualizations of identified fragments. Additionally, Proteo-SAFARI includes a nonnegative least-squares fitting approach to determine the contributions of various hydrogen shifted fragment ions ( + 1, + 1, - 1, - 2) observed in UVPD mass spectra which exhibit overlapping isotopic distributions.
View Article and Find Full Text PDFAlzheimers Dement
December 2024
Emory University School of Medicine, Atlanta, GA, USA.
Background: The microtubule-associated Tau gene (MAPT) undergoes alternative splicing to produce isoforms with varying combinations of microtubule-binding region (MTBR) repeats (3R, 4R). The MTBR is the predominant region that forms paired helical filaments and neurofibrillary tangles fibrils in disease. Alzheimer's disease (AD) is a mixed Tauopathy containing both 3R and 4R isoforms.
View Article and Find Full Text PDFBackground: Bile acids (BA) are steroids regulating nutrient absorption, energy metabolism, and mitochondrial function, and serve as important signaling molecules with a role in the gut-brain axis. The composition of BAs in humans changes with diet type and health status, which is well documented with a few known bile acids. In this study, we leveraged a new BA-specific spectral library curated in the Dorrestein lab at UCSD to expand the pool of detected BAs in Alzheimer-related LC-MS/MS datasets and provide links to dietary profiles and AD markers.
View Article and Find Full Text PDFAlzheimers Dement
December 2024
Tokyo Metropolitan Geriatric Hospital and Institute of Gerontology, Itabashi-ku, Tokyo, Japan.
Background: Although amyloid deposition in brain is one of the hallmark pathological features of Alzheimer's disease (AD), the upstream events and its molecular environment in AD brain remain largely unknown. Recent advances in analytical methods such as mass spectrometry can provide the cutting-edge tools to unveil the AD pathogenesis at molecular and atomic level.
Method: In order to gain the comprehensive information about AD pathology at molecular level, postmortem brain sections of AD patients were analyzed by the hybrid molecular imaging methods composed of the conventional histological analyses, matrix assisted laser desorption ionization mass spectrometry imaging (MALDI-MSI) for small molecules, laser ablation inductively coupled plasma mass spectrometry (LA-ICP-MS) imaging for metals, and particle induced X-ray emission (PIXE) imaging for elements.
Nat Commun
January 2025
Gilbert S. Omenn Department of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI, USA.
Data-independent acquisition has become a widely used strategy for peptide and protein quantification in liquid chromatography-tandem mass spectrometry-based proteomics studies. The integration of ion mobility separation into data-independent acquisition analysis, such as the diaPASEF technology available on Bruker's timsTOF platform, further improves the quantification accuracy and protein depth achievable using data-independent acquisition. We introduce diaTracer, a spectrum-centric computational tool optimized for diaPASEF data.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!