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Mass Spectrometry Reviews

Şule Yılmaz, Genet A Shiferaw, Josep Rayo, Anastassios Economou, Lennart Martens, Elien Vandermarliere
Chemical cross-linking analyzed by mass spectrometry (XL-MS) has become an important tool in unravelling protein structure, dynamics, and complex formation. Because the analysis of cross-linked proteins with mass spectrometry results in specific computational challenges, many computational tools have been developed to identify cross-linked peptides from mass spectra and subsequently interpret the identified cross-links within their structural context. In this review, we will provide an overview of the different tools that are currently available to tackle the computational part of an XL-MS experiment...
March 12, 2018: Mass Spectrometry Reviews
Zian Lin, Zongwei Cai
Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) is an excellent analytical technique for rapid and sensitive analysis of macromolecules such as polymers and proteins. However, the main drawback of MALDI-TOF MS is its difficulty to detect small molecules with mass below 700 Da because of the intensive interference from MALDI matrix in the low mass region. In recent years there has been considerable interest in developing matrix-free laser desorption/ionization by using nanostructured substrates to substitute the conventional organic matrices, which is often referred as surface-assisted laser desorption/ionization time-of-flight mass spectrometry (SALDI-TOF MS)...
March 6, 2018: Mass Spectrometry Reviews
Liang Cui, Haitao Lu, Yie Hou Lee
In the past decade, advances in liquid chromatography-mass spectrometry (LC-MS) have revolutionized untargeted metabolomics analyses. By mining metabolomes more deeply, researchers are now primed to uncover key metabolites and their associations with diseases. The employment of untargeted metabolomics has led to new biomarker discoveries and a better mechanistic understanding of diseases with applications in precision medicine. However, many major pertinent challenges remain. First, compound identification has been poor, and left an overwhelming number of unidentified peaks...
February 27, 2018: Mass Spectrometry Reviews
Frederik Lermyte, Dirk Valkenborg, Joseph A Loo, Frank Sobott
In recent years, electron capture (ECD) and electron transfer dissociation (ETD) have emerged as two of the most useful methods in mass spectrometry-based protein analysis, evidenced by a considerable and growing body of literature. In large part, the interest in these methods is due to their ability to induce backbone fragmentation with very little disruption of noncovalent interactions which allows inference of information regarding higher order structure from the observed fragmentation behavior. Here, we review the evolution of electron-based dissociation methods, and pay particular attention to their application in "native" mass spectrometry, their mechanism, determinants of fragmentation behavior, and recent developments in available instrumentation...
February 9, 2018: Mass Spectrometry Reviews
Paul Vouros, Dominic Desiderio
No abstract text is available yet for this article.
March 2018: Mass Spectrometry Reviews
Gabriella Pinto, Marko Radulovic, Jasminka Godovac-Zimmermann
The Redox Code involves specific, reversible oxidative changes in proteins that modulate protein tertiary structure, interactions, trafficking, and activity, and hence couple the proteome to the metabolic/oxidative state of cells. It is currently a major focus of study in cell biology. Recent studies of dynamic cellular spatial reorganization with MS-based subcellular-spatial-razor proteomics reveal that protein constituents of many subcellular structures, including mitochondria, the endoplasmic reticulum, the plasma membrane, and the extracellular matrix, undergo changes in their subcellular abundance/distribution in response to oxidative stress...
January 2018: Mass Spectrometry Reviews
Daniel James Wilkinson
Over a century ago, Frederick Soddy provided the first evidence for the existence of isotopes; elements that occupy the same position in the periodic table are essentially chemically identical but differ in mass due to a different number of neutrons within the atomic nucleus. Allied to the discovery of isotopes was the development of some of the first forms of mass spectrometers, driven forward by the Nobel laureates JJ Thomson and FW Aston, enabling the accurate separation, identification, and quantification of the relative abundance of these isotopes...
January 2018: Mass Spectrometry Reviews
Suresh Kumar Aggarwal
The manuscript reviews the various mass spectrometric techniques for analysis and chemical studies of Americium. These methods include thermal ionization mass spectrometry (TIMS), and inductively coupled plasma source mass spectrometry (ICPMS) for the determination of Am isotope ratios and concentration in nuclear fuel samples of interest in nuclear technology, and in complex biological and environmental samples. Ultra-sensitive mass spectrometric techniques of resonance-ionization mass spectrometry (RIMS), and accelerator-based mass spectrometry (AMS) are also discussed...
January 2018: Mass Spectrometry Reviews
Valentina Peruzzo, Matteo Andrea Chiurato, Monica Favaro, Patrizia Tomasin
Metal alkoxides are metal-organic compounds characterized by the presence of MOC bonds (M = metal). Their chemistry seems to be, in principle, relatively simple but the number of possible reactant species arising as a consequence of their behavior is very remarkable. The physico-chemical properties of metal alkoxides are determined by many different parameters, the most important ones being the electronegativity of the metal, the ramification of the ligand, and the acidity of the corresponding alcohol...
January 2018: Mass Spectrometry Reviews
Tianfang Wang, T T Nha Tran, Hayley J Andreazza, Daniel Bilusich, Craig S Brinkworth, John H Bowie
It is now 25 years since we commenced the study of the negative-ion fragmentations of peptides and we have recently concluded this research with investigations of the negative-ion chemistry of most post-translational functional groups. Our first negative-ion peptide review (Bowie, Brinkworth, & Dua, 2002) dealt with the characteristic backbone fragmentations and side-chain cleavages from (M-H)- ions of underivatized peptides, while the second (Bilusich & Bowie, 2009) included negative-ion backbone cleavages for Ser and Cys and some initial data on some post-translational groups including disulfides...
January 2018: Mass Spectrometry Reviews
Qiwei Zhang, Zack Li, Yawei Wang, Qi Zheng, Jianjun Li
Sialic acids are a family of structurally unique and negatively charged nine-carbon sugars, normally found at the terminal positions of glycan chains on glycoproteins and glycolipids. The glycosylation of proteins is a universal post-translational modification in eukaryotic species and regulates essential biological functions, in which the most common sialic acid is N-acetyl-neuraminic acid (2-keto-5-acetamido-3,5-dideoxy-D-glycero-D-galactononulopyranos-1-onic acid) (Neu5NAc). Because of the properties of sialic acids under general mass spectrometry (MS) conditions, such as instability, ionization discrimination, and mixed adducts, the use of MS in the analysis of protein sialoglycosylation is still challenging...
December 11, 2017: Mass Spectrometry Reviews
Michal Fárník, Jozef Lengyel
Nanometer-size particles such as ultrafine aerosol particles, ice nanoparticles, water nanodroplets, etc, play an important, however, not yet fully understood role in the atmospheric chemistry and physics. These species are often composed of water with admixture of other atmospherically relevant molecules. To mimic and investigate such particles in laboratory experiments, mixed water clusters with atmospherically relevant molecules can be generated in molecular beams and studied by various mass spectrometric methods...
November 27, 2017: Mass Spectrometry Reviews
Hemi Luan, Xian Wang, Zongwei Cai
Metabolomics seeks to take a "snapshot" in a time of the levels, activities, regulation and interactions of all small molecule metabolites in response to a biological system with genetic or environmental changes. The emerging development in mass spectrometry technologies has shown promise in the discovery and quantitation of neuroactive small molecule metabolites associated with gut microbiota and brain. Significant progress has been made recently in the characterization of intermediate role of small molecule metabolites linked to neural development and neurodegenerative disorder, showing its potential in understanding the crosstalk between gut microbiota and the host brain...
November 12, 2017: Mass Spectrometry Reviews
Thomas De Vijlder, Dirk Valkenborg, Filip Lemière, Edwin P Romijn, Kris Laukens, Filip Cuyckens
The identification of unknown molecules has been one of the cornerstone applications of mass spectrometry for decades. This tutorial reviews the basics of the interpretation of electrospray ionization-based MS and MS/MS spectra in order to identify small-molecule analytes (typically below 2000 Da). Most of what is discussed in this tutorial also applies to other atmospheric pressure ionization methods like atmospheric pressure chemical/photoionization. We focus primarily on the fundamental steps of MS-based structural elucidation of individual unknown compounds, rather than describing strategies for large-scale identification in complex samples...
November 9, 2017: Mass Spectrometry Reviews
Robert Moulder, Santosh D Bhosale, David R Goodlett, Riitta Lahesmaa
Over the past decade, chemical labeling with isobaric tandem mass tags, such as isobaric tags for relative and absolute quantification reagents (iTRAQ) and tandem mass tag (TMT) reagents, has been employed in a wide range of different clinically orientated serum and plasma proteomics studies. In this review the scope of these works is presented with attention to the areas of research, methods employed and performance limitations. These applications have covered a wide range of diseases, disorders and infections, and have implemented a variety of different preparative and mass spectrometric approaches...
November 9, 2017: Mass Spectrometry Reviews
Miao Qu, Bo An, Shichen Shen, Ming Zhang, Xiaomeng Shen, Xiaotao Duan, Joseph P Balthasar, Jun Qu
In the last decade, the advancement of liquid chromatography mass spectrometry (LC/MS) techniques has enabled their broad application in protein characterization, both quantitatively and qualitatively. Owing to certain important merits of LC/MS techniques (e.g., high selectivity, flexibility, and rapid method development), LC/MS assays are often deemed as preferable alternatives to conventional methods (e.g., ligand-binding assays) for the analysis of protein biotherapeutics. At the discovery and development stages, LC/MS is generally employed for two purposes absolute quantification of protein biotherapeutics in biological samples and qualitative characterization of proteins...
November 2017: Mass Spectrometry Reviews
David Z Keifer, Martin F Jarrold
In single-molecule mass spectrometry, the mass of each ion is measured individually; making it suitable for the analysis of very large, heterogeneous objects that cannot be analyzed by conventional means. A range of single-molecule mass spectrometry techniques has been developed, including time-of-flight with cryogenic detectors, a quadrupole ion trap with optical detection, single-molecule Fourier transform ion cyclotron resonance, charge detection mass spectrometry, quadrupole ion traps coupled to charge detector plates, and nanomechanical oscillators...
November 2017: Mass Spectrometry Reviews
Miao Wang, Chunyan Wang, Xianlin Han
Lipidomics is rapidly expanding because of the great facilitation of recent advances in, and novel applications of, electrospray ionization mass spectrometry techniques. The greatest demands have been for successful quantification of lipid classes, subclasses, and individual molecular species in biological samples at acceptable accuracy. This review addresses the selection of internal standards in different methods for accurate quantification of individual lipid species. The principles of quantification with electrospray ionization mass spectrometry are first discussed to recognize the essentials for quantification...
November 2017: Mass Spectrometry Reviews
Piliang Hao, Sunil S Adav, Xavier Gallart-Palau, Siu Kwan Sze
Protein deamidation has been proposed to represent a "molecular clock" that progressively disrupts protein structure and function in human degenerative diseases and natural aging. Importantly, this spontaneous process can also modify therapeutic proteins by altering their purity, stability, bioactivity, and antigenicity during drug synthesis and storage. Deamidation occurs non-enzymatically in vivo, but can also take place spontaneously in vitro, hence artificial deamidation during proteomic sample preparation can hamper efforts to identify and quantify endogenous deamidation of complex proteomes...
November 2017: Mass Spectrometry Reviews
Dirk Nolting, Robert Malek, Alexander Makarov
This review is devoted to trapping mass spectrometry wherein ions are confined by electromagnetic fields for prolonged periods of time within limited volume, with mass measurement taking place within the same volume. Three major types of trapping mass spectrometers are discussed, specifically radiofrequency ion trap, Fourier transform ion cyclotron resonance and Orbitrap. While these three branches are intricately interwoven with each other over their recent history, they also differ greatly in their fundamentals, roots and historical origin...
October 30, 2017: Mass Spectrometry Reviews
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