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Author: Stacy D. Sherrod
Publisher:
ISBN:
Category :
Languages : en
Pages :
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Book Description
Imaging mass spectrometry (MS) analysis allows scientists the ability to obtain spatial and chemical information of analytes on a wide variety of surfaces. The ability to image biological analytes is an important tool in many areas of life science research, including: the ability to map pharmaceutical drugs in targeted tissue, to spatially determine the expression profile of specific proteins in healthy vs. diseased tissue states, and to rapidly interrogate biomolecular microarrays. However, there are several avenues for improving the imaging MS experiment for biological samples. Three significant directions this work addresses include: (1) reducing chemical noise and increasing analyte identification by developing sample preparation methodologies, (2) improving the analytical figures of merit (i.e., spatial resolution, analysis time) by implementing a spatially dynamic optical system, and (3) increasing both mass spectral resolution and ion detection sensitivity by modifying a commercial time-of-flight (TOF) MS. Firstly, sample methodology schemes presented in these studies consist of obtaining both?top-down? and?bottom-up? information. In that, both intact mass and peptide mass fingerprinting data can be obtained to increase protein identification. This sample methodology was optimized on protein microarrays in preparation for bio tissue analysis. Other work consists of optimizing novel sample preparation strategies for hydrated solid-supported lipid bilayer studies. Sample methods incorporating nanomaterials for laser desorption/ionization illustrate the ability to perform selective ionization of specific analytes. Specifically, our results suggest that silver nanoparticles facilitate the selective ionization of olefin containing species (e.g., steroids, vitamins). Secondly, an advanced optical design incorporating a spatially dynamic optical scheme allows for laser beam expansion, homogenization, collimation, shaping, and imaging. This spatially dynamic optical system allows user defined beam shapes, decreases analysis times associated with mechanical movement of the sample stage, and is capable of increasing the MS limits of detection by simultaneously irradiating multiple spots. Lastly, new data acquisition strategies (multiple anode detection schemes) were incorporated into a commercial time-of-flight mass spectrometer to increase both sensitivity and resolution in a matrix assisted laser desorption/ionization mass spectrometer. The utility of this technique can be applied to many different samples, where high mass spectral resolution allows for increased mass measurement accuracy.
Author: Stacy D. Sherrod
Publisher:
ISBN:
Category :
Languages : en
Pages :
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Book Description
Imaging mass spectrometry (MS) analysis allows scientists the ability to obtain spatial and chemical information of analytes on a wide variety of surfaces. The ability to image biological analytes is an important tool in many areas of life science research, including: the ability to map pharmaceutical drugs in targeted tissue, to spatially determine the expression profile of specific proteins in healthy vs. diseased tissue states, and to rapidly interrogate biomolecular microarrays. However, there are several avenues for improving the imaging MS experiment for biological samples. Three significant directions this work addresses include: (1) reducing chemical noise and increasing analyte identification by developing sample preparation methodologies, (2) improving the analytical figures of merit (i.e., spatial resolution, analysis time) by implementing a spatially dynamic optical system, and (3) increasing both mass spectral resolution and ion detection sensitivity by modifying a commercial time-of-flight (TOF) MS. Firstly, sample methodology schemes presented in these studies consist of obtaining both?top-down? and?bottom-up? information. In that, both intact mass and peptide mass fingerprinting data can be obtained to increase protein identification. This sample methodology was optimized on protein microarrays in preparation for bio tissue analysis. Other work consists of optimizing novel sample preparation strategies for hydrated solid-supported lipid bilayer studies. Sample methods incorporating nanomaterials for laser desorption/ionization illustrate the ability to perform selective ionization of specific analytes. Specifically, our results suggest that silver nanoparticles facilitate the selective ionization of olefin containing species (e.g., steroids, vitamins). Secondly, an advanced optical design incorporating a spatially dynamic optical scheme allows for laser beam expansion, homogenization, collimation, shaping, and imaging. This spatially dynamic optical system allows user defined beam shapes, decreases analysis times associated with mechanical movement of the sample stage, and is capable of increasing the MS limits of detection by simultaneously irradiating multiple spots. Lastly, new data acquisition strategies (multiple anode detection schemes) were incorporated into a commercial time-of-flight mass spectrometer to increase both sensitivity and resolution in a matrix assisted laser desorption/ionization mass spectrometer. The utility of this technique can be applied to many different samples, where high mass spectral resolution allows for increased mass measurement accuracy.
Author: Sreeraj Gopi
Publisher:
ISBN: 9781774911129
Category : High resolution spectroscopy
Languages : en
Pages : 0
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Book Description
Presents knowledge on the technologies and applications of high-resolution mass spectrometry in different areas of analysis. Discusses instrumentation techniques and presents research on diverse uses of HRMS in clinical testing: therapeutic drug designing and development; quality management systems; analysis of pesticides; etc.
Author: Kris Gevaert
Publisher: Springer Nature
ISBN: 1071634577
Category : Science
Languages : en
Pages : 337
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Book Description
This detailed volume explores contemporary techniques in mass spectrometry-based proteomics. After covering overall proteome coverage and the cellular surfaceome, the book delves into proximity-induced biotinylation, abduction of protein complexes in viral-like particles, and thermal proteome profiling, as well as protocols for identifying protein N-terminal acetylation, protein processing by proteases, protein N-glycosylation, and protein phosphorylation. The book also collects chapters on automated preparation of clinical samples, the analysis of formalin-fixed paraffin-embedded samples, protocols for the isolation of extracellular vesicles and for the monitoring of selected protein modifications in clinical samples, and, finally, structural proteomics. Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step and readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Mass Spectrometry-Based Proteomics serves as an ideal guide to its subject for both novices in the field of proteomics as well as specialists.
Author:
Publisher:
ISBN:
Category :
Languages : en
Pages : 0
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Book Description
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: Mary S. Lipton
Publisher: Humana Press
ISBN: 9781607611042
Category : Science
Languages : en
Pages : 470
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Book Description
When the last edition of this book was published in 2000, the field of proteomics was in its infancy. At that time, multidimensional liquid chromatographic separations were being introduced as an alternative to traditional gel-based techniques for separating complex protein and peptide mixtures prior to mass spectrometric detection. Today, this approach – referred to as shotgun proteomics – is considered routine for lar- scale global analyses of protein mixtures. Now in its adolescence, proteomics is fundamentally transforming biological and medical research. Much of this transformation can be attributed to technological advancements, particularly in mass spectrometry. Much wider accessibility of hi- resolution and mass measurement accuracy instrumentation in recent years has ini- ated a new revolution in the field by providing more reliable data and shifting the focus from cataloging proteins to precisely quantifying changes in protein abundance over time and in response to stimuli. Advanced mass spectrometers and novel ion d- sociation schemes such as electron transfer/capture dissociation make it possible to venture boldly into the maze of protein posttranslational modifications, which are an integral component of understanding functional proteomics in the spatial and t- poral domains. Another area that has benefited from these advancements is top-down proteomics, an emerging method essential for characterizing various protein variants that has potentially high impact in biomedical research.
Author: Nader Rifai
Publisher: Elsevier
ISBN: 0128160640
Category : Science
Languages : en
Pages : 218
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Book Description
Principles and Applications of Clinical Mass Spectrometry: Small Molecules, Peptides, and Pathogens is a concise resource for quick implementation of mass spectrometry methods in clinical laboratory work. Focusing on the practical use of these techniques, the first half of the book covers principles of chromatographic separations, principles and types of mass spectrometers, and sample preparation for analysis; the second half outlines the main applications of this technology within clinical laboratory settings, including determination of small molecules and peptides, as well as pathogen identification. A thorough yet succinct guide to using mass spectrometry technology in the clinical laboratory, Principles and Applications of Clinical Mass Spectrometry: Small Molecules, Peptides, and Pathogens is an essential resource for chemists, pharmaceutical and biotech researchers, certain government agencies, and standardization groups. - Provides concrete examples of the main applications of mass spectrometry technology - Describes current capabilities of the LC- and MS-based analytical methods - Details methods for successful analytical work in the field
Author: Ingvar Eidhammer
Publisher: Wiley-Interscience
ISBN: 9780470512975
Category : Medical
Languages : en
Pages : 0
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Book Description
Proteomics is the study of the subsets of proteins present in different parts of an organism and how they change with time and varying conditions. Mass spectrometry is the leading technology used in proteomics, and the field relies heavily on bioinformatics to process and analyze the acquired data. Since recent years have seen tremendous developments in instrumentation and proteomics-related bioinformatics, there is clearly a need for a solid introduction to the crossroads where proteomics and bioinformatics meet. Computational Methods for Mass Spectrometry Proteomics describes the different instruments and methodologies used in proteomics in a unified manner. The authors put an emphasis on the computational methods for the different phases of a proteomics analysis, but the underlying principles in protein chemistry and instrument technology are also described. The book is illustrated by a number of figures and examples, and contains exercises for the reader. Written in an accessible yet rigorous style, it is a valuable reference for both informaticians and biologists. Computational Methods for Mass Spectrometry Proteomics is suited for advanced undergraduate and graduate students of bioinformatics and molecular biology with an interest in proteomics. It also provides a good introduction and reference source for researchers new to proteomics, and for people who come into more peripheral contact with the field.
Author: Chad R. Weisbrod
Publisher:
ISBN:
Category :
Languages : en
Pages : 196
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Book Description
Traditionally and most commonly, accurate mass measurement is utilized to restrict peptide candidate search space on the precursor level to impart greater specificity in large peptide sequence databases. While use of accurate mass measurement is effective for discovery based proteomics, here we present novel applications of accurate mass measurement in proteomics to make further use of this expensive (monetarily and in time) acquisition attribute. This work began with the coupling and testing of a hybrid dual cell linear ion trap mass spectrometer (Velos) to a 7T Fourier transform ion cyclotron resonance (FTICR) mass spectrometer. This combination provides high speed, efficient ion accumulation with the high resolution and mass accuracy of FTICR. Using this mass spectrometer (Velos-FT) and an LTQ-Orbitrap it was shown theoretically and empirically that high resolution product ion spectra alone can be utilized to detect and quantify peptides. A DIA acquisition and data processing pipeline called, FT-All Reaction Monitoring (FT-ARM), was designed to exploit this observation. Direct similarities of FT-ARM to targeted proteomics data allow for discovery and targeted proteomics to be conducted in a single pass with little to no assay development. A search algorithm developed to score and assess data acquired using this strategy enabled quantitation into the attomole range and enabled identification within a complex background matrix. Specificity of the peptide assignment is attributed to the requirement of the simultaneous observation of a minimum number of product ions from the target peptide at a required mass measurement accuracy. Real-time informatics analysis during mass spectrometry acquisition can serve to simplify post-acquisition analysis and more importantly, focus measurements on ions more likely to yield the desired information. Real-time informatics applied to engineered, cleavable cross-linkers allows known mass relationships to be used to direct subsequent experiments. Peptides released from cross-linked complexes can be directly targeted for MS3 acquisition to obtain sequence information within a single LC/MS/MS acquisition. This new mass spectrometry method called Real-time Analysis for Cross-linked peptide Technology (ReACT) has been developed to enable assignment of cross-linked peptides "on-the-fly". Using ReACT, 708 unique cross-linked (
Author: Gary Siuzdak
Publisher: Elsevier
ISBN: 0080535844
Category : Science
Languages : en
Pages : 179
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Book Description
If you investigate biological systems and might use mass spectrometry in your research but need to know more about it, this book is for you. It introduces the fundamental concepts of mass spectrometry and how mass spectrometers work. It also presents recent advancements particularly interesting to bio-researchers in an easy-to-understand manner that does not require extensive background in chemistry, math, or physics. - Glossary of basic terms - Abundant illustrations - Examples of applications - Practical tips on using mass spectrometric techniques - Useful for peptide, protein, oligonucleotide, and carbohydrate analysis - Simplified description of mass spectrometry including: - Matrix-Assisted Laser Desorption/Ionization (MALDI) - Electrospray Ionization (ESI) - Fast Atom/Ion Bombardment (FAB)
Author:
Publisher:
ISBN:
Category : Medicine
Languages : en
Pages : 1812
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Book Description
