Selected Reaction Monitoring Mass Spectrometry Srm Ms In Proteomics
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| Author | : Mahmud Hossain |
| Publisher | : Springer Nature |
| Total Pages | : 283 |
| Release | : 2020-09-26 |
| Genre | : Science |
| ISBN | : 3030534332 |
Covering a wide-ranging facet of a “gold-standard” targeted mass spectrometry (MS) method for the consistent detection and accurate quantification of preselected proteins in complex biological matrices, Selected Reaction Monitoring Mass Spectrometry (SRM-MS) in Proteomics: A Comprehensive View describes: The knowledge-based development of highly efficient SRM methodology including assay workflow, selection of proteins, peptides, transitions and its validation, and quality assessment Available bioinformatic tools – for both pre-acquisition method development and post-MS acquisition data analysis and data repositories Various relative and absolute quantification techniques SRM-MS’ widespread applications in biomarker development and in clinical studies, as well as in the analysis of various posttranslational modifications (PTMs) Current challenges and contemporary trends to overcome those difficulties In addition, it features the historical development of modern-day mass spectrometry with its vivid applications and also covers basic MS instrumentation, ionization techniques, and various proteomics approaches. Comprehensive discussion, extensive references at the end of each chapter, and the list of review articles in the bibliography offer invaluable resources for advanced readings. Researchers from the undergraduate to postgraduate level and beyond in both academic or industry settings studying and working on mass spectrometry and/or proteomics will benefit from this book.
| Author | : Michael Kinter |
| Publisher | : Springer Science & Business Media |
| Total Pages | : 76 |
| Release | : 2013-09-17 |
| Genre | : Medical |
| ISBN | : 1461486661 |
A key experiment in biomedical research is monitoring the expression of different proteins in order to detect changes that occur in biological systems under different experimental conditions. The method that is most widely used is the Western blot analysis. While Western blot is a workhorse in laboratories studying protein expression and has several advantages, it also has a number of significant limitations. In particular, the method is semi-quantitative with limited dynamic range. Western blot focuses on a single protein per sample with only a small number of representative samples analyzed in an experiment. New quantitative tools have been needed for some time to at least supplement, & possibly replace, the Western blot. Mass spectrometric methods have begun to compete with Western blot for routine quantitative analyses of proteins. One of these methods is based on the tandem mass spectrometry technique of selected reaction monitoring (SRM), which is also called multiple reaction monitoring (MRM). Selected reaction monitoring is actually an older tandem mass spectrometry technique, first described in the late 70s, that is widely utilized in the quantitative analysis of small molecules like drugs & metabolites. The use of selected reaction monitoring for the quantitative analysis of proteins has a number of advantages. Most importantly, it is fundamentally quantitative with a wide dynamic range. The output of the analysis is a numerical result that can range over several orders of magnitude. Other advantages include sufficient specificity & sensitivity to detect low abundance proteins in complex mixtures. Finally, selected reaction monitoring can be multiplexed to allow the quantitative analysis of relatively large numbers of proteins in a single sample in a single experiment. This Brief will explain both the theoretical & experimental details of the selected reaction monitoring experiment as it is applied to proteins.
| Author | : Conrad Bessant |
| Publisher | : Royal Society of Chemistry |
| Total Pages | : 429 |
| Release | : 2016-11-15 |
| Genre | : Science |
| ISBN | : 1782626735 |
The field of proteomics has developed rapidly over the past decade nurturing the need for a detailed introduction to the various informatics topics that underpin the main liquid chromatography tandem mass spectrometry (LC-MS/MS) protocols used for protein identification and quantitation. Proteins are a key component of any biological system, and monitoring proteins using LC-MS/MS proteomics is becoming commonplace in a wide range of biological research areas. However, many researchers treat proteomics software tools as a black box, drawing conclusions from the output of such tools without considering the nuances and limitations of the algorithms on which such software is based. This book seeks to address this situation by bringing together world experts to provide clear explanations of the key algorithms, workflows and analysis frameworks, so that users of proteomics data can be confident that they are using appropriate tools in suitable ways.
| Author | : Claire E Eyers |
| Publisher | : Royal Society of Chemistry |
| Total Pages | : 391 |
| Release | : 2014 |
| Genre | : Science |
| ISBN | : 1849738084 |
As a component of post-genome science, the field of proteomics has assumed great prominence in recent years. Whereas quantitative analyses focussed initially on relative quantification, a greater emphasis is now placed on absolute quantification and consideration of proteome dynamics. Coverage of the topic of quantitative proteomics requires consideration both of the analytical fundamentals of quantitative mass spectrometry and the specific demands of the problem being addressed. Quantitative Proteomics aims to outline the state of the art in mass spectrometry-based quantitative proteomics, describing recent advances and current limitations in the instrumentation used, together with the various methods employed for generating high quality data. Details on both strategies describing how stable isotope labelling can be applied and methods for performing quantitative analysis of proteins in a label-free manner are given. The utility of these strategies to understanding cellular protein dynamics are then exemplified with chapters looking at spatial proteomics, dynamics of protein function as determined by quantifying changes in protein post-translational modification and protein turnover. Finally, a key application of these techniques to biomarker discovery and validation is presented, together with the rapidly developing area of quantitative analysis of protein-based foodstuffs. This exemplary book is essential reading for analytical and biological mass spectrometrists working in proteomics research, as well as those undertaking either fundamental or clinical-based investigations with an interest in understanding protein dynamics and/or biomarker assessment.
| Author | : Jorge Barros-Velázquez |
| Publisher | : Royal Society of Chemistry |
| Total Pages | : 384 |
| Release | : 2021-03-23 |
| Genre | : Science |
| ISBN | : 1839163011 |
Presenting an up-to-date review of the state-of-the-art and main applications of omics technologies to current hot topics in food sciences, this book is divided into four convenient sections. The first section represents an introduction to the development of foodomics and will provide a general overview of DNA-based and protein-based methods. The second section is focused on the main applications of omics to food safety issues, such as chemical hazards, foodborne pathogens, phages, food authentication or GMO detection. The third section is focused on specific food groups and how omics have revolutionized the investigation of dairy and meat products, seafood, agricultural and fermented food products. Finally, the fourth section is devoted to the link between foodomics and health: hot topics such as nutrimetabolomics, food allergy or probiotics are reviewed here. The book brings together work from top international scientists to produce the most significant academic book for some years on omics and food for a broad audience. It presents unique features not covered so far by other books, such as a detailed description of different strategies and applications of omics techniques to many food sectors and provides a welcome addition to the cutting-edge literature in this area for researchers and professionals in food science and food chemistry.
| Author | : |
| Publisher | : |
| Total Pages | : 0 |
| Release | : 2012 |
| Genre | : |
| ISBN | : |
The work described herein spans two disparate topics: 1) the use of a high resolution and accurate mass analyzer to facilitate targeted proteomic methods, and 2) the development and applications of novel instrumentation for high resolution gas chromatography/mass spectrometry. While disparate, a common theme of a high resolution and accurate mass analyzer, the Orbitrap, ties the work together into, broadly, a treatise on the benefits of high resolution and accurate mass measurements in mass spectrometric research. In Chapter 1, I present an introduction on the Orbitrap mass analyzer and motivate the need for high resolution and accurate mass measurements in mass spectrometry. I will discuss the theory of Orbitrap operation, as well as the practical factors that may enhance or limit its performance. In Chapter 2, I delve into the field of targeted proteomics with the introduction of the "parallel reaction monitoring" (PRM) analysis paradigm using a bench-top quadrupole-Orbitrap LC/MS. While targeted proteomics is usually the domain of low resolution but highly sensitive mass analyzers, I demonstrate the utility of high resolution with a direct comparison to the "gold-standard" triple-quadrupole MS-based selected reaction monitoring (SRM) approach. This PRM approach has already generated much interest in the proteomics community since its publication. In Chapters 3 through 5, I transition to GC/MS, another field dominated by low resolution and fast scanning mass analyzers. In Chapter 3, I detail the construction and characterization of a proof-of-principle instrument for high resolution GC/MS built using an electron transfer dissociation (ETD)-enabled quadrupole linear ion trap (QLT)-Orbitrap MS. While the performance of this instrument was hindered by its design, the benefits of the Orbitrap for unambiguous elemental composition assignment to small molecules were clear, and further development was deemed warranted. In Chapter 4, I detail that further development in the design and construction of a dedicated, applications-grade bench-top quadrupole-Orbitrap GC/MS. The application of this instrument to the non-targeted characterization of unknown metabolites is presented in Chapter 5. Additionally in Chapter 5, I introduce a new method for data-dependent acquisition termed "molecular-ion directed acquisition", which aims to maximize the information content from non-targeted tandem MS in metabolomic studies
| Author | : Katrin Marcus |
| Publisher | : Humana Press |
| Total Pages | : 539 |
| Release | : 2012-06-08 |
| Genre | : Science |
| ISBN | : 9781617798849 |
Protein modifications and changes made to them, as well as the quantities of expressed proteins, can define the various functional stages of the cell. Accordingly, perturbations can lead to various diseases and disorders. As a result, it has become paramount to be able to detect and monitor post-translational modifications and to measure the abundance of proteins within the cell with extreme sensitivity. While protein identification is an almost routine requirement nowadays, reliable techniques for quantifying unmodified proteins (including those that escape detection under standard conditions, such as protein isoforms and membrane proteins) is not routine. Quantitative Methods in Proteomics gives a detailed survey of topics and methods on the principles underlying modern protein analysis, from statistical issues when planning proteomics experiments, to gel-based and mass spectrometry-based applications. The quantification of post-translational modifications is also addressed, followed by the “hot” topics of software and data analysis, as well as various overview chapters which provide a comprehensive overview of existing methods in quantitative proteomics. Written in the successful Methods in Molecular BiologyTM series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible protocols, and notes on troubleshooting and avoiding known pitfalls. Authoritative and easily accessible, Quantitative Methods in Proteomics serves as a comprehensive and competent overview of the important and still growing field of quantitative proteomics.
| Author | : Kazuhiro Imai |
| Publisher | : CRC Press |
| Total Pages | : 314 |
| Release | : 2013-08-05 |
| Genre | : Science |
| ISBN | : 9814316512 |
This book focuses on the advantages and disadvantages of each of the commonly used quantitative proteomic methods in terms of accuracy, sensitivity, and reproducibility. It also concentrates on the effective applications of these methods that resulted in many discoveries of the role of the proteins expressed in living cells and biological fluids. The first part of the book focuses on the description of advantages and disadvantages of each of the commonly used quantitative proteomic methods in terms of accuracy, sensitivity, and, especially, reproducibility. The second part of the book focuses on providing concise descriptions of the effective applications of these methods to demonstrate how they have resulted in many important discoveries of the roles of the proteins expressed in living cells.
| Author | : Tiffany Siegel Porta |
| Publisher | : Royal Society of Chemistry |
| Total Pages | : 541 |
| Release | : 2021-12-03 |
| Genre | : Science |
| ISBN | : 1839162414 |
This book gathers knowledge about matrix-assisted laser desorption ionisation (MALDI) mass spectrometry imaging for postgraduate and professional researchers in academia and in industry where it has direct application to clinical research.
| Author | : Mahmood Aliofkhazraei |
| Publisher | : BoD – Books on Demand |
| Total Pages | : 284 |
| Release | : 2017-06-07 |
| Genre | : Science |
| ISBN | : 9535132237 |
Mass spectrometry is an analytical technique that can be used for the structural characterization and quantification of a wide range of molecules. The technique is extensively used by chemists for the analysis of small and volatile organic compounds. Mass spectrometry has long been an important technique for the identification of materials ranging from pure compounds to complex mixtures. Mass spectrometry can be used to determine molecular weight of compounds or using different ionization conditions, can provide more structural details through the analysis of fragmentation patterns. This level of detail can be attained for pure compounds and some mixtures. Mass spectrometry can also be combined with separation techniques such as gas chromatography or liquid chromatography to allow more complex mixtures to be examined. These hyphenated techniques provide a range of options for the characterization of complex materials.
