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Science (New York, N.Y.) Apr 2006Mass spectrometry is a central analytical technique for protein research and for the study of biomolecules in general. Driven by the need to identify, characterize, and... (Review)
Review
Mass spectrometry is a central analytical technique for protein research and for the study of biomolecules in general. Driven by the need to identify, characterize, and quantify proteins at ever increasing sensitivity and in ever more complex samples, a wide range of new mass spectrometry-based analytical platforms and experimental strategies have emerged. Here we review recent advances in mass spectrometry instrumentation in the context of current and emerging research strategies in protein science.
Topics: Mass Spectrometry; Peptide Mapping; Proteins; Proteome; Proteomics; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
PubMed: 16614208
DOI: 10.1126/science.1124619 -
Analytical and Bioanalytical Chemistry Oct 2007The quantification of differences between two or more physiological states of a biological system is among the most important but also most challenging technical tasks... (Review)
Review
The quantification of differences between two or more physiological states of a biological system is among the most important but also most challenging technical tasks in proteomics. In addition to the classical methods of differential protein gel or blot staining by dyes and fluorophores, mass-spectrometry-based quantification methods have gained increasing popularity over the past five years. Most of these methods employ differential stable isotope labeling to create a specific mass tag that can be recognized by a mass spectrometer and at the same time provide the basis for quantification. These mass tags can be introduced into proteins or peptides (i) metabolically, (ii) by chemical means, (iii) enzymatically, or (iv) provided by spiked synthetic peptide standards. In contrast, label-free quantification approaches aim to correlate the mass spectrometric signal of intact proteolytic peptides or the number of peptide sequencing events with the relative or absolute protein quantity directly. In this review, we critically examine the more commonly used quantitative mass spectrometry methods for their individual merits and discuss challenges in arriving at meaningful interpretations of quantitative proteomic data.
Topics: Electronic Data Processing; Isotope Labeling; Mass Spectrometry; Peptides; Proteins; Proteome; Proteomics; Reference Standards
PubMed: 17668192
DOI: 10.1007/s00216-007-1486-6 -
Mass Spectrometry Reviews May 2021The boost of research output in lipidomics during the last decade is tightly linked to improved instrumentation in mass spectrometry. Associated with this trend is the... (Review)
Review
The boost of research output in lipidomics during the last decade is tightly linked to improved instrumentation in mass spectrometry. Associated with this trend is the shift from low resolution-toward high-resolution lipidomics platforms. This review article summarizes the state of the art in the lipidomics field with a particular focus on the merits of high mass resolution. Following some theoretical considerations on the benefits of high mass resolution in lipidomics, it starts with a historical perspective on lipid analysis by sector instruments and moves further to today's instrumental approaches, including shotgun lipidomics, liquid chromatography-mass spectrometry, matrix-assisted laser desorption ionization-time-of-flight, and imaging lipidomics. Subsequently, several data processing and data analysis software packages are critically evaluated with all their pros and cons. Finally, this article emphasizes the importance and necessity of quality standards as the field evolves from its pioneering phase into a mature and robust omics technology and lists various initiatives for improving the applicability of lipidomics. © 2020 The Authors. Mass Spectrometry Reviews published by John Wiley & Sons Ltd. Mass Spec Rev.
Topics: Chromatography, Liquid; Humans; Lipidomics; Lipids; Mass Spectrometry; Software; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
PubMed: 32233039
DOI: 10.1002/mas.21627 -
Analytical Chemistry Jan 2018
Review
Topics: Animals; Clinical Chemistry Tests; Humans; Mass Spectrometry; Single-Cell Analysis
PubMed: 29155564
DOI: 10.1021/acs.analchem.7b04733 -
Annual Review of Analytical Chemistry... 2015Developments in forensic mass spectrometry tend to follow, rather than lead, the developments in other disciplines. Examples of techniques having forensic potential born... (Review)
Review
Developments in forensic mass spectrometry tend to follow, rather than lead, the developments in other disciplines. Examples of techniques having forensic potential born independently of forensic applications include ambient ionization, imaging mass spectrometry, isotope ratio mass spectrometry, portable mass spectrometers, and hyphenated chromatography-mass spectrometry instruments, to name a few. Forensic science has the potential to benefit enormously from developments that are funded by other means, if only the infrastructure and personnel existed to adopt, validate, and implement the new technologies into casework. Perhaps one unique area in which forensic science is at the cutting edge is in the area of chemometrics and the determination of likelihood ratios for the evaluation of the weight of evidence. Such statistical techniques have been developed most extensively for ignitable-liquid residue analyses and isotope ratio analysis. This review attempts to capture the trends, motivating forces, and likely impact of developing areas of forensic mass spectrometry, with the caveat that none of this research is likely to have any real impact in the forensic community unless: (a) The instruments developed are turned into robust black boxes with red and green lights for positives and negatives, respectively, or (b) there are PhD graduates in the workforce who can help adopt these sophisticated techniques.
Topics: Forensic Medicine; Humans; Mass Spectrometry
PubMed: 26070716
DOI: 10.1146/annurev-anchem-071114-040335 -
Mass Spectrometry Reviews Jan 2022Laser ionization mass spectrometry (LIMS) was one of the first practical methods developed for in situ analysis of the surfaces of solid samples. This review will... (Review)
Review
Laser ionization mass spectrometry (LIMS) was one of the first practical methods developed for in situ analysis of the surfaces of solid samples. This review will encompass several aspects related to this analytical method. First, we will discuss the process of laser ionization, the influence of the laser type on its performance, and imaging capabilities of this method. In the second chapter, we will follow the historic development of LIMS instrumentation. After a brief overview of the first-generation instruments developed in 1960-1990 years, we will discuss in detail more recent designs, which appeared during the last 2-3 decades. In the last part of our review, we will cover the recent applications of LIMS for surface analysis. These applications include various types of analyses of solid inorganic, organic, and heterogeneous samples, often in combination with depth profiling and imaging capability.
Topics: Lasers; Mass Spectrometry; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
PubMed: 33169900
DOI: 10.1002/mas.21669 -
Current Protocols in Protein Science Nov 2010Mass spectrometry is an indispensable tool for peptide and protein analysis owing to its speed, sensitivity, and versatility. It can be used to determine amino acid...
Mass spectrometry is an indispensable tool for peptide and protein analysis owing to its speed, sensitivity, and versatility. It can be used to determine amino acid sequences of peptides, and to characterize a wide variety of post-translational modifications such as phosphorylation and glycosylation. Mass spectrometry can also be used to determine absolute and relative protein quantities, and can identify and quantify thousands of proteins from complex samples, which makes it an extremely powerful tool for systems biology studies. The main goals of this unit are to familiarize peptide and protein chemists and biologists with the types of mass spectrometers that are appropriate for the majority of their analytical needs, to describe the kinds of experiments that can be performed with these instruments on a routine basis, and to discuss the kinds of information that these experiments provide.
Topics: Amino Acid Sequence; Chemistry Techniques, Analytical; Glycosylation; Mass Spectrometry; Peptide Mapping; Peptides; Phosphorylation; Protein Processing, Post-Translational; Proteins; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Tandem Mass Spectrometry
PubMed: 21104985
DOI: 10.1002/0471140864.ps1601s62 -
Biochimica Et Biophysica Acta. Proteins... Jan 2022Native mass spectrometry (MS), the analysis of proteins and protein complexes from solutions that stabilize native solution structures, is a rapidly expanding area.... (Review)
Review
Native mass spectrometry (MS), the analysis of proteins and protein complexes from solutions that stabilize native solution structures, is a rapidly expanding area. There is strong evidence supporting the retention of proteins' native folds in the absence of solvent under the experimental timescales of MS experiments. Therefore, instrumentation has been developed to use gas-phase native-like protein ions to exploit the speed, sensitivity, and selectivity of mass spectrometry approaches to solve emerging problems in structural biology. This article reviews some of the recent advances and applications in gas-phase instrumentation for structural proteomics.
Topics: Mass Spectrometry; Multiprotein Complexes
PubMed: 34653668
DOI: 10.1016/j.bbapap.2021.140732 -
The Analyst Jan 2016A common feature of ribonucleic acids (RNAs) is that they can undergo a variety of chemical modifications. As nearly all of these chemical modifications result in an... (Review)
Review
A common feature of ribonucleic acids (RNAs) is that they can undergo a variety of chemical modifications. As nearly all of these chemical modifications result in an increase in the mass of the canonical nucleoside, mass spectrometry has long been a powerful approach for identifying and characterizing modified RNAs. Over the past several years, significant advances have been made in method development and software for interpreting tandem mass spectra resulting in approaches that can yield qualitative and quantitative information on RNA modifications, often at the level of sequence specificity. We discuss these advances along with instrumentation developments that have increased our ability to extract such information from relatively complex biological samples. With the increasing interest in how these modifications impact the epitranscriptome, mass spectrometry will continue to play an important role in bioanalytical investigations revolving around RNA.
Topics: Mass Spectrometry; Nucleosides; RNA
PubMed: 26501195
DOI: 10.1039/c5an01797a -
Analytical Chemistry Jun 1994
Review
Topics: Carbohydrates; Fourier Analysis; Mass Spectrometry; Peptides; Proteins
PubMed: 8092481
DOI: 10.1021/ac00084a024