Andries P. Bruins: A Revolution for Modern Mass Spectrometry

2010 ◽  
Vol 16 (1) ◽  
pp. vii-viii
Author(s):  
Andrea Raffaelli ◽  
Alessandro Saba
Keyword(s):  
Mass Spectrometry ◽  
Modern Mass

scholarly journals Gas-Phase Fragmentation of Cyclic Oligosaccharides in Tandem Mass Spectrometry

Molecules ◽  
2019 ◽  
Vol 24 (12) ◽  
pp. 2226 ◽  
Author(s):  
Alexander O. Chizhov ◽  
Yury E. Tsvetkov ◽  
Nikolay E. Nifantiev
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Gas Phase ◽  
Structure Elucidation ◽  
Mass Spectra ◽  
Food Additives ◽  
Tandem Mass ◽  
Modern Mass ◽  
Gas Phase Fragmentation ◽  
Different Sources

Modern mass spectrometry, including electrospray and MALDI, is applied for analysis and structure elucidation of carbohydrates. Cyclic oligosaccharides isolated from different sources (bacteria and plants) have been known for decades and some of them (cyclodextrins and their derivatives) are widely used in drug design, as food additives, in the construction of nanomaterials, etc. The peculiarities of the first- and second-order mass spectra of cyclic oligosaccharides (natural, synthetic and their derivatives and modifications: cyclodextrins, cycloglucans, cyclofructans, cyclooligoglucosamines, etc.) are discussed in this minireview.

scholarly journals A Pragmatic Guide to Enrichment Strategies for Mass Spectrometry-based Glycoproteomics

2020 ◽  
pp. mcp.R120.002277 ◽  
Author(s):  
Nicholas M Riley ◽  
Carolyn R Bertozzi ◽  
Sharon J Pitteri
Keyword(s):  
Mass Spectrometry ◽  
Molecular Biology ◽  
Chemical Biology ◽  
Hydrophilic Interaction Chromatography ◽  
Porous Graphitic Carbon ◽  
Graphitic Carbon ◽  
Hydrophilic Interaction ◽  
Chemical Coupling ◽  
Modern Mass ◽  
Enrichment Strategy

Glycosylation is a prevalent, yet heterogeneous modification with a broad range of implications in molecular biology. This heterogeneity precludes enrichment strategies that can be universally beneficial for all glycan classes. Thus, choice of enrichment strategy has profound implications on experimental outcomes. Here we review common enrichment strategies used in modern mass spectrometry (MS)-based glycoproteomic experiments, including lectins and other affinity chromatographies, hydrophilic interaction chromatography (HILIC) and its derivatives, porous graphitic carbon (PGC), reversible and irreversible chemical coupling strategies, and chemical biology tools that often leverage bioorthogonal handles. Interest in glycoproteomics continues to surge as MS instrumentation and software improve, so this review aims to help equip researchers with necessary information to choose appropriate enrichment strategies that best complement these efforts.

scholarly journals Trends in the Design of New Isobaric Labeling Reagents for Quantitative Proteomics

Molecules ◽  
2019 ◽  
Vol 24 (4) ◽  
pp. 701 ◽  
Author(s):  
Remigiusz Bąchor ◽  
Mateusz Waliczek ◽  
Piotr Stefanowicz ◽  
Zbigniew Szewczuk
Keyword(s):  
Mass Spectrometry ◽  
Quantitative Proteomics ◽  
Chemical Properties ◽  
High Energy ◽  
Tandem Mass ◽  
Peptide Molecule ◽  
Wide Range ◽  
Potential Applications ◽  
Isobaric Tag ◽  
Modern Mass

Modern mass spectrometry is one of the most frequently used methods of quantitative proteomics, enabling determination of the amount of peptides in a sample. Although mass spectrometry is not inherently a quantitative method due to differences in the ionization efficiency of various analytes, the application of isotope-coded labeling allows relative quantification of proteins and proteins. Over the past decade, a new method for derivatization of tryptic peptides using isobaric labels has been proposed. The labels consist of reporter and balanced groups. They have the same molecular weights and chemical properties, but differ in the distribution of stable heavy isotopes. These tags are designed in such a way that during high energy collision induced dissociation (CID) by tandem mass spectrometry, the isobaric tag is fragmented in the specific linker region, yielding reporter ions with different masses. The mass shifts among the reporter groups are compensated by the balancing groups so that the overall mass is the same for all forms of the reagent. Samples of peptides are labeled with the isobaric mass tags in parallel and combined for analysis. Quantification of individual peptides is achieved by comparing the intensity of reporter ions in the tandem mass (MS/MS) spectra. Isobaric markers have found a wide range of potential applications in proteomics. However, the currently available isobaric labeling reagents have some drawbacks, such as high cost of production, insufficient selectivity of the derivatization, and relatively limited enhancement of sensitivity of the analysis. Therefore, efforts have been devoted to the development of new isobaric markers with increased usability. The search for new isobaric markers is focused on developing a more selective method of introducing a tag into a peptide molecule, increasing the multiplexicity of markers, lowering the cost of synthesis, and increasing the sensitivity of measurement by using ionization tags containing quaternary ammonium salts. Here, the trends in the design of new isobaric labeling reagents for quantitative proteomics isobaric derivatization strategies in proteomics are reviewed, with a particular emphasis on isobaric ionization tags. The presented review focused on different types of isobaric reagents used in quantitative proteomics, their chemistry, and advantages offer by their application.

scholarly journals Ion traps in modern mass spectrometry

2017 ◽  
Vol 38 (2) ◽  
pp. 150-168 ◽  
Author(s):  
Dirk Nolting ◽  
Robert Malek ◽  
Alexander Makarov
Keyword(s):  
Mass Spectrometry ◽  
Ion Traps ◽  
Modern Mass

scholarly journals Modern mass spectrometry for synthetic biology and structure-based discovery of natural products

2016 ◽  
Vol 33 (8) ◽  
pp. 942-950 ◽  
Author(s):  
Matthew T. Henke ◽  
Neil L. Kelleher
Keyword(s):  
Mass Spectrometry ◽  
Natural Products ◽  
Synthetic Biology ◽  
Modern Mass ◽  
Natural Products Discovery

This highlight serves as a primer for those curious about the abilities of mass spectrometry for natural products discovery and engineering.

Direct Analysis of Elastomer Compounds by Soft Ionization, Tandem (MS/MS) and High Resolution (AC-MS) Mass Spectrometry

1995 ◽  
Vol 68 (5) ◽  
pp. 783-793 ◽  
Author(s):  
Robert P. Lattimer
Keyword(s):  
Mass Spectrometry ◽  
Thermoplastic Polyurethane ◽  
High Sensitivity ◽  
High Specificity ◽  
Mass Spectrometric ◽  
Spectrometric Analysis ◽  
Tandem Ms ◽  
Organic Additives ◽  
Soft Ionization ◽  
Modern Mass

Abstract In recent years very effective mass spectrometric methods have been developed for direct polymer compound analysis. The high sensitivity, high specificity, and superb mixture analysis capabilities of modern mass spectrometry make it an invaluable tool in the polymer industry, particularly for qualitative analysis (chemical identification) of organic additives as well as polymeric components. “Survey” mass spectra obtained with soft ionization methods — field ionization (FI-MS) and chemical ionization (CI-MS) — provide diagnostic overviews of chemical composition. The supplemental tandem (MS/MS) and atomic composition (AC-MS) techniques are used to make specific identifications of various organic ingredients. This report describes the direct mass spectrometric analysis of three different elastomer compounds. Organic additives, including curatives, were identified via thermal desorption methods in a commercial EPDM bearing as well as a diene rubber V-belt. The composition of a commercial thermoplastic polyurethane was determined via pyrolysis (Py-CI-MS). These problem-solving examples illustrate the very effective role that mass spectrometry can play in the industrial polymer analysis laboratory.

scholarly journals The Plant PTM Viewer, a central resource exploring plant protein modifications. From site-seeing to protein function

2018 ◽  
Author(s):  
Patrick Willems ◽  
Alison Horne ◽  
Sofie Goormachtig ◽  
Ive De Smet ◽  
Alexander Botzki ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Posttranslational Modifications ◽  
Protein Function ◽  
Protein Sequences ◽  
Specific Protein ◽  
Specific Information ◽  
Active Site Residues ◽  
Functional Protein ◽  
Protein Modifications ◽  
Modern Mass

SUMMARYPosttranslational modifications (PTMs) of proteins are central in any kind of cellular signaling. Modern mass spectrometry technologies enable comprehensive identification and quantification of various PTMs. Given the increased number and types of mapped protein modifications, a database is necessary that simultaneouly integrates and compares site-specific information for different PTMs, especially in plants for which the available PTM data are poorly catalogued. Here, we present the Plant PTM Viewer (http://www.psb.ugent.be/PlantPTMViewer), an integrative PTM resource that comprises approximately 200,000 PTM sites for 17 types of protein modifications in plant proteins from five different species. The Plant PTM Viewer provides the user with a protein sequence overview in which the experimentally evidenced PTMs are highlighted together with functional protein domains or active site residues. The PTM sequence search tool can query PTM combinations in specific protein sequences, whereas the PTM BLAST tool searches for modified protein sequences to detect conserved PTMs in homologous sequences. Taken together, these tools facilitate to assume the role and potential interplay of PTMs in specific proteins or within a broader systems biology context. The Plant PTM Viewer is an open repository that allows submission of mass spectrometry-based PTM data to remain at pace with future PTM plant studies.

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