Advancing Intact Protein Analysis By Top Down Mass Spectrometry

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Advancing Intact Protein Analysis by Top-down Mass Spectrometry

Author : Bifan Chen
Publisher :
ISBN 13 :
Total Pages : 215 pages
Book Rating : 4.:/5 (123 download)

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Book Synopsis Advancing Intact Protein Analysis by Top-down Mass Spectrometry by : Bifan Chen

Download or read book Advancing Intact Protein Analysis by Top-down Mass Spectrometry written by Bifan Chen and published by . This book was released on 2019 with total page 215 pages. Available in PDF, EPUB and Kindle. Book excerpt: The study of proteins is critical for understanding cellular functions at the molecular level. Top-down mass spectrometry (MS) has emerged as a premier tool for global and comprehensive analysis of proteoforms. The top-down approach retains intact mass information, providing a "bird's-eye" view of the proteome and allowing for identification of novel proteoforms, in-depth sequence characterization, and quantification of disease associated post-translational modifications (PTMs). However, many technical challenges still exist. The research described here involves analytical development in top-down MS, particularly in the areas of enrichment, separation, and characterization of samples ranging from standard proteins and complex lysates, to large therapeutic biomolecules. Chapter 1 provides an introduction and review of recent advances in different aspects of top-down proteomics. Chapters 2 and 3 are related to the study of intact phosphoproteins. Specifically, chapter 2 describes the use of functionalized nanoparticles for enrichment and the subsequent coupling of online liquid chromatography (LC)-MS for characterizing endogenous phosphoproteins from complex cell lysates. Chapter 3 investigates how phosphorylation moieties might influence the efficiency of electron capture dissociation (ECD). Chapters 4 and 5 focus on the development of hydrophobic interaction chromatography (HIC) that could be coupled online directly with MS and its applications to therapeutic molecules (monoclonal antibodies). Chapter 6 describes a middle-down approach to obtain multi-attribute of both cysteine and lysine conjugated antibody-drug conjugates, which overcomes some current challenges using HIC-MS and the top-down approach. Overall, these analytical developments expand the toolbox of the top-down approach and generally facilitate the analysis of intact proteins.

Internal Fragments in Top-down and Middle-down Mass Spectrometry

Author : Benqian Wei
Publisher :
ISBN 13 :
Total Pages : 0 pages
Book Rating : 4.:/5 (14 download)

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Book Synopsis Internal Fragments in Top-down and Middle-down Mass Spectrometry by : Benqian Wei

Download or read book Internal Fragments in Top-down and Middle-down Mass Spectrometry written by Benqian Wei and published by . This book was released on 2023 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: The interrogation of protein structure, especially identifying and localizing post-translational modifications (PTMs) and sites of ligand/small molecule binding, is crucial for understanding protein function in biological systems. In particular, the rapid increase of the use and development of therapeutic monoclonal antibodies (mAbs) and antibody-drug conjugates (ADCs) for human health have necessitated the advancement of efficient and accurate analytical methods. Top-down and middle-down mass spectrometry (TD- and MD-MS) have become prominent analytical tools for protein characterization. However, obtaining complete protein sequence coverage by TD-/MD-MS can be limiting, particularly for proteins greater than 30 kDa, e.g., mAbs and ADCs. My dissertation research explores the utility of internal fragments, which are largely ignored by the MS community as they are difficult to assign, from both fundamental and application perspectives, for more efficient and comprehensive protein sequence, structure, and PTM characterization. On the fundamental side, we demonstrated a relationship between internal fragments and conventional terminal fragments. A better understanding of the fundamental formation mechanism of internal fragments aids the development of sequencing algorithms to assign internal fragments more accurately and reliably. On the application side, we started by analyzing standard disulfide-intact proteins using TD-MS, in which assigning internal fragments helped achieve near complete sequence coverage, and obtain disulfide bond position and connectivity information. This encouraged us to apply TD-MS on proteins of therapeutic significance, i.e., mAbs and ADCs, which are extremely complex disulfide-intact proteins. Incorporating internal fragments analysis allowed us to achieve the highest sequence coverage to date on an intact mAb by TD-MS, and enabled the access of important PTM information and drug binding information on intact ADCs. We then expanded this application by applying MD-MS on reduced mAbs and ADCs. Analyzing internal fragments in MD-MS helped us achieve comprehensive characterization of mAbs and ADCs which is a significant improvement from TD-MS and is comparable to the results obtained from the routinely utilized bottom-up peptide mapping method. Lastly, we demonstrated that assigning internal fragments generated by collision-based fragmentation also helps deliver higher-order structure information of multi-subunit protein assemblies. In summary, this dissertation work contributes to advancing the technique and instrumentation surrounding TD- and MD-MS workflows to achieve better characterization of proteins, especially biotherapeutics, and identification of specific proteoforms.

Direct Analysis of Intact Proteins from Microorganisms Using Top Down Mass Spectrometry

Author : Fanyu Meng
Publisher :
ISBN 13 :
Total Pages : 174 pages
Book Rating : 4.:/5 (551 download)

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Book Synopsis Direct Analysis of Intact Proteins from Microorganisms Using Top Down Mass Spectrometry by : Fanyu Meng

Download or read book Direct Analysis of Intact Proteins from Microorganisms Using Top Down Mass Spectrometry written by Fanyu Meng and published by . This book was released on 2003 with total page 174 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Methodologies and Applications for the Analysis of Intact Proteins and Protein-ligand Interactions by Top-down Mass Spectrometry

Author : Michael Nshanian
Publisher :
ISBN 13 :
Total Pages : 175 pages
Book Rating : 4.:/5 (15 download)

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Book Synopsis Methodologies and Applications for the Analysis of Intact Proteins and Protein-ligand Interactions by Top-down Mass Spectrometry by : Michael Nshanian

Download or read book Methodologies and Applications for the Analysis of Intact Proteins and Protein-ligand Interactions by Top-down Mass Spectrometry written by Michael Nshanian and published by . This book was released on 2018 with total page 175 pages. Available in PDF, EPUB and Kindle. Book excerpt: The advent of top-down protein mass spectrometry (MS), or direct analysis of intact proteins forgoing proteolysis, has transformed the field of protein mass spectrometry, ushering in a new era of protein identification and characterization together with a new set of challenges. The analysis of intact proteins and their direct fragmentation in tandem (MS/MS) mode helps overcome the "inference" problem associated with peptide-based bottom-up proteomics; that is, correctly assigning given peptide fragments and their modifications to the intact protein from which they originated. Despite its many advantages, however, the top-down approach requires extensive sample fractionation and suffers from low sensitivity but much progress has been made. From recently-developed cross-linked polyacrylamide gels, from which intact proteins can be more easily recovered, to the discovery of reagents that enhance protein charging in electrospray ionization (ESI), there have been considerable gains in detection and sensitivity, offering the potential for a more complete and accurate characterization of a "proteoform": the full complement of the combinatorial possibilities that could arise from a given gene product. Top-down MS also includes the study of proteins in their native or native-like states. This is especially important in characterizing disease-related proteins, particularly in the context of protein aggregation. Native MS, using electron-capture dissociation (ECD) and ion mobility spectrometry (IMS), enables the study of protein-inhibitor complexes in the gas phase, offering structural insight into stoichiometry, site of inhibitor binding and mechanism of inhibition. In addition, intact analysis and electron-based fragmentation enable the detection of thermally-labile post-translational modifications like phosphorylation, known to play key regulatory roles in shifting proteins towards cytotoxic states. Top-down method developments in protein recovery, separation and supercharging have led to improvements in detection and sensitivity, while top-down MS applications to structural characterization of disease-related proteins have shed more light on the mechanisms of cytotoxic aggregation, offering greater promise of therapeutic development.

Proteoform Identification

Author : Liangliang Sun
Publisher : Humana
ISBN 13 : 9781071623275
Total Pages : 0 pages
Book Rating : 4.6/5 (232 download)

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Book Synopsis Proteoform Identification by : Liangliang Sun

Download or read book Proteoform Identification written by Liangliang Sun and published by Humana. This book was released on 2023-06-18 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: This volume discusses the latest mass spectrometry (MS)-based technologies for proteoform identification, characterization, and quantification. Some of the topics covered in this book include sample preparation, proteoform separation, proteoform gas-phase fragmentation, and bioinformatics tools for MS data analysis. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Cutting-edge and comprehensive, Proteoform Identification: Methods and Protocols is a valuable resource for researchers in both academia and the biopharmaceutical industry who are interested in proteoform analysis using MS.

Developing Top-down Mass Spectrometry for Intact Protein Identification in the Chromatographic Timescale

Author : Rajeswari Lakshmanan
Publisher :
ISBN 13 :
Total Pages : 225 pages
Book Rating : 4.:/5 (847 download)

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Book Synopsis Developing Top-down Mass Spectrometry for Intact Protein Identification in the Chromatographic Timescale by : Rajeswari Lakshmanan

Download or read book Developing Top-down Mass Spectrometry for Intact Protein Identification in the Chromatographic Timescale written by Rajeswari Lakshmanan and published by . This book was released on 2012 with total page 225 pages. Available in PDF, EPUB and Kindle. Book excerpt: Protein identification by top-down mass spectrometry based methods yield intact mass of the proteins and indicate the presence of post-translational modifications (PTMs) and/or isoforms. Currently, the methods employed for top-down protein identification are performed using instruments with dual mass analyzers and are based on fragmenting isolated charge states, which greatly reduces the duty cycle of the instrument. High throughput top-down methods are required for protein identification in complex sample mixtures. We demonstrate the capability to perform intact protein identifications in a single-stage time-of-flight mass spectrometer during protein elution from a liquid chromatography (LC) column. In addition, we have developed a new data-independent fragmentation method known as `Continuous Accumulation of Selected Ions-Collisionally Activated Dissociation' (CASI-CAD) to fragment multiple charge states of the protein simultaneously for the purpose of identification in the LC timescale. CASI-CAD is performed without any precursor selection and thus, the duty-cycle of the instrument is not lowered. Both these methods unambiguously identified all the proteins in the human proteasome complex used for method development. The presence of PTMs and N-terminal modifications were also characterized for the proteins in this complex. Supercharging reagents are known for their ability to enhance the multiple charging of proteins during electrospray ionization (ESI). This improves the mass measurement accuracy and fragmentation efficiency of proteins during ESI-MS. Currently, the mechanism behind supercharging is unknown. We have analyzed different supercharging reagents under a variety of solvent conditions to probe the mechanisms behind supercharging. In addition, the supercharging ability of sulfolane was utilized for proteins eluting from a column by adding the reagent to the LC solvents. Furthermore, reagent introduction in the vapor phase increased the signal intensity for intact proteins eluting from a column when compared to experiments performed without the reagent. These methods presented here are efficient top-down means to address complex samples in the chromatographic timescale.

Quantitative Methods in Proteomics

Author : Katrin Marcus
Publisher : Humana Press
ISBN 13 : 9781617798849
Total Pages : 539 pages
Book Rating : 4.7/5 (988 download)

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Book Synopsis Quantitative Methods in Proteomics by : Katrin Marcus

Download or read book Quantitative Methods in Proteomics written by Katrin Marcus and published by Humana Press. This book was released on 2012-06-08 with total page 539 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.

Integrated Computational and Experimental Platform for Characterizing Protein Isoforms and PTMs in Microbial Systems by Top-down FT-ICR Mass Spectrometry

Download Integrated Computational and Experimental Platform for Characterizing Protein Isoforms and PTMs in Microbial Systems by Top-down FT-ICR Mass Spectrometry PDF Online Free

Author : Heather Marie Connelly
Publisher :
ISBN 13 :
Total Pages : 251 pages
Book Rating : 4.:/5 (718 download)

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Book Synopsis Integrated Computational and Experimental Platform for Characterizing Protein Isoforms and PTMs in Microbial Systems by Top-down FT-ICR Mass Spectrometry by : Heather Marie Connelly

Download or read book Integrated Computational and Experimental Platform for Characterizing Protein Isoforms and PTMs in Microbial Systems by Top-down FT-ICR Mass Spectrometry written by Heather Marie Connelly and published by . This book was released on 2006 with total page 251 pages. Available in PDF, EPUB and Kindle. Book excerpt: The goals of this dissertation research were to develop an integrated computational and experimental platform for characterizing protein isoforms and post translational modifications (PTMs) in microbial systems by top-down FT-ICR mass spectrometry. To accomplish this goal, we employed methodologies of microbial growth, intact protein and protein complex extractions, followed by sample preparation and then progressed to identification of the instrumentation needed to integrate the top-down and bottom-up proteomics methodologies used in these studies. Emphasis is placed on the development of integrated top-down and bottom-up informatics and the challenges faced in the integration of these two large mass spectrometry data sets and extraction of relevant biological data. We then illustrate how top-down and bottom-up methods can be applied to the analysis of complex protein mixtures, protein complexes, and microbial proteomes. Through the work of this dissertation we have contributed to the advancement of top-down proteomics by providing an experimental platform which will aid in the analysis of intact proteins and their associated PTMs and isoforms, as well as providing a computational method that allows for the integration of top-down and bottom-up data sets.

Advanced New Technologies for Protein Analysis by Mass Spectrometry

Author : Pui Yiu Lam
Publisher :
ISBN 13 :
Total Pages : 408 pages
Book Rating : 4.:/5 (11 download)

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Book Synopsis Advanced New Technologies for Protein Analysis by Mass Spectrometry by : Pui Yiu Lam

Download or read book Advanced New Technologies for Protein Analysis by Mass Spectrometry written by Pui Yiu Lam and published by . This book was released on 2018 with total page 408 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Neuroproteomics

Author : Oscar Alzate
Publisher : CRC Press
ISBN 13 : 1420076264
Total Pages : 356 pages
Book Rating : 4.4/5 (2 download)

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Book Synopsis Neuroproteomics by : Oscar Alzate

Download or read book Neuroproteomics written by Oscar Alzate and published by CRC Press. This book was released on 2009-10-26 with total page 356 pages. Available in PDF, EPUB and Kindle. Book excerpt: In this, the post-genomic age, our knowledge of biological systems continues to expand and progress. As the research becomes more focused, so too does the data. Genomic research progresses to proteomics and brings us to a deeper understanding of the behavior and function of protein clusters. And now proteomics gives way to neuroproteomics as we beg

Protein Analysis using Mass Spectrometry

Author : Mike S. Lee
Publisher : John Wiley & Sons
ISBN 13 : 1119359368
Total Pages : 282 pages
Book Rating : 4.1/5 (193 download)

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Book Synopsis Protein Analysis using Mass Spectrometry by : Mike S. Lee

Download or read book Protein Analysis using Mass Spectrometry written by Mike S. Lee and published by John Wiley & Sons. This book was released on 2017-05-26 with total page 282 pages. Available in PDF, EPUB and Kindle. Book excerpt: Presents Practical Applications of Mass Spectrometry for Protein Analysis and Covers Their Impact on Accelerating Drug Discovery and Development Covers both qualitative and quantitative aspects of Mass Spectrometry protein analysis in drug discovery Principles, Instrumentation, Technologies topics include MS of peptides, proteins, and ADCs , instrumentation in protein analysis, nanospray technology in MS protein analysis, and automation in MS protein analysis Details emerging areas from drug monitoring to patient care such as Identification and validation of biomarkers for cancer, targeted MS approaches for biomarker validation, biomarker discovery, and regulatory perspectives Brings together the most current advances in the mass spectrometry technology and related method in protein analysis

Proteomics Sample Preparation

Author : Jörg von Hagen
Publisher : John Wiley & Sons
ISBN 13 : 3527644695
Total Pages : 498 pages
Book Rating : 4.5/5 (276 download)

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Book Synopsis Proteomics Sample Preparation by : Jörg von Hagen

Download or read book Proteomics Sample Preparation written by Jörg von Hagen and published by John Wiley & Sons. This book was released on 2011-08-24 with total page 498 pages. Available in PDF, EPUB and Kindle. Book excerpt: This long-awaited first guide to sample preparation for proteomics studies overcomes a major bottleneck in this fast growing technique within the molecular life sciences. By addressing the topic from three different angles -- sample, method and aim of the study -- this practical reference has something for every proteomics researcher. Following an introduction to the field, the book looks at sample preparation for specific techniques and applications and finishes with a section on the preparation of sample types. For each method described, a summary of the pros and cons is given, as well as step-by-step protocols adaptable to any specific proteome analysis task.

Hydrogen Exchange Mass Spectrometry of Proteins

Author : David D. Weis
Publisher : John Wiley & Sons
ISBN 13 : 1118616499
Total Pages : 422 pages
Book Rating : 4.1/5 (186 download)

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Book Synopsis Hydrogen Exchange Mass Spectrometry of Proteins by : David D. Weis

Download or read book Hydrogen Exchange Mass Spectrometry of Proteins written by David D. Weis and published by John Wiley & Sons. This book was released on 2016-03-21 with total page 422 pages. Available in PDF, EPUB and Kindle. Book excerpt: Hydrogen exchange mass spectrometry is widely recognized for its ability to probe the structure and dynamics of proteins. The application of this technique is becoming widespread due to its versatility for providing structural information about challenging biological macromolecules such as antibodies, flexible proteins and glycoproteins. Although the technique has been around for 25 years, this is the first definitive book devoted entirely to the topic. Hydrogen Exchange Mass Spectrometry of Proteins: Fundamentals, Methods and Applications brings into one comprehensive volume the theory, instrumentation and applications of Hydrogen Exchange Mass Spectrometry (HX-MS) - a technique relevant to bioanalytical chemistry, protein science and pharmaceuticals. The book provides a solid foundation in the basics of the technique and data interpretation to inform readers of current research in the method, and provides illustrative examples of its use in bio- and pharmaceutical chemistry and biophysics In-depth chapters on the fundamental theory of hydrogen exchange, and tutorial chapters on measurement and data analysis provide the essential background for those ready to adopt HX-MS. Expert users may advance their current understanding through chapters on methods including membrane protein analysis, alternative proteases, millisecond hydrogen exchange, top-down mass spectrometry, histidine exchange and method validation. All readers can explore the diversity of HX-MS applications in areas such as ligand binding, membrane proteins, drug discovery, therapeutic protein formulation, biocomparability, and intrinsically disordered proteins.

New Front-end Separation Approaches for Top-down Proteomics

Author : Eli Larson
Publisher :
ISBN 13 :
Total Pages : 0 pages
Book Rating : 4.:/5 (141 download)

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Book Synopsis New Front-end Separation Approaches for Top-down Proteomics by : Eli Larson

Download or read book New Front-end Separation Approaches for Top-down Proteomics written by Eli Larson and published by . This book was released on 2023 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: Top-down mass spectrometry (MS) and top-down proteomics have become indispensable tools to characterize and identify unique proteoforms. Proteoforms are defined as all protein products of a single gene, including splicing variants, mutants, and post-translationally modified forms. Although the development of new MS capabilities has exploded in recent years, the comparative underdevelopment of intact protein separations and data processing solutions has prevented full realization of the benefits of top-down. To address these challenges, I have developed new front-end separation approaches for top-down proteomics, beginning with targeted separations for multi-attribute analysis of antibody-drug conjugates (ADCs) and later developing an online two-dimensional liquid chromatography (2DLC) method to expand global proteome coverage by top-down proteomics. Chapter 1 focuses on recent advances in front-end separations and data processing solutions for top-down proteomics and introduces top-down applications to antibody-based therapeutic analysis. Chapter 2 and chapter 3 detail new targeted separation approaches for monoclonal antibodies and ADCs. Chapter 2 reports reversed phase liquid chromatography (RPLC) coupled to high-resolution Fourier transform ion cyclotron resonance MS for top-down analysis of a reduced cysteine-linked ADC. Chapter 3 details the development of a native complex-down workflow using trapped ion mobility spectrometry-MS with a cysteine-linked ADC and parent mAb under non-denaturing conditions (Chapter 3). Chapter 4 reports a new software package designed to address the challenges associated with native top-down proteomics, MASH Native. Chapter 5 focuses on the development of a new online 2DLC method coupling serial size exclusion and RPLC to expand global top-down proteome coverage, with application to human heart extract. Appendix I reports a shotgun proteomic approach to characterize the impact of splicing factor RNA binding motif 20 knockout on the rat heart proteome and identifies targets for follow-up analysis by top-down proteomics. The developed techniques detailed here will address key challenges to front-end separation in the field of top-down proteomics, expanding analytical capabilities for future targeted and discovery studies.

Development of Advanced Optics and High Resolution Instrumentation for Mass Spectrometry Based Proteomics

Author : Stacy D. Sherrod
Publisher :
ISBN 13 :
Total Pages : pages
Book Rating : 4.:/5 (69 download)

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Book Synopsis Development of Advanced Optics and High Resolution Instrumentation for Mass Spectrometry Based Proteomics by : Stacy D. Sherrod

Download or read book Development of Advanced Optics and High Resolution Instrumentation for Mass Spectrometry Based Proteomics written by Stacy D. Sherrod and published by . This book was released on 2010 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.

Protein and Peptide Analysis by LC-MS

Author : Thomas Letzel
Publisher : Royal Society of Chemistry
ISBN 13 : 1849733147
Total Pages : 195 pages
Book Rating : 4.8/5 (497 download)

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Book Synopsis Protein and Peptide Analysis by LC-MS by : Thomas Letzel

Download or read book Protein and Peptide Analysis by LC-MS written by Thomas Letzel and published by Royal Society of Chemistry. This book was released on 2011-07-22 with total page 195 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book is the first example in presenting LC-MS strategies for the analysis of peptides and proteins with detailed information and hints about the needs and problems described from experts on-the-job. The best advantage is -for sure- the practical insight of experienced analysts into their novel protein analysis techniques. Readers starting in 'Proteomics' should be able to repeat each experiment with own equipment and own protein samples, like clean-up, direct protein analysis, after (online) digest, with modifications and others. Furthermore, the reader will learn more about strategies in protein analysis, like quantitative analysis, industrial standards, functional analysis and more.

Characterization of Protein Therapeutics using Mass Spectrometry

Author : Guodong Chen
Publisher : Springer Science & Business Media
ISBN 13 : 1441978623
Total Pages : 408 pages
Book Rating : 4.4/5 (419 download)

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Book Synopsis Characterization of Protein Therapeutics using Mass Spectrometry by : Guodong Chen

Download or read book Characterization of Protein Therapeutics using Mass Spectrometry written by Guodong Chen and published by Springer Science & Business Media. This book was released on 2014-07-08 with total page 408 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book highlights current approaches and future trends in the use of mass spectrometry to characterize protein therapies. As one of the most frequently utilized analytical techniques in pharmaceutical research and development, mass spectrometry has been widely used in the characterization of protein therapeutics due to its analytical sensitivity, selectivity, and specificity. This book begins with an overview of mass spectrometry techniques as related to the analysis of protein therapeutics, structural identification strategies, quantitative approaches, followed by studies involving characterization of process related protein drug impurities/degradants, metabolites, higher order structures of protein therapeutics. Both general practitioners in pharmaceutical research and specialists in analytical sciences will benefit from this book that details step-by-step approaches and new strategies to solve challenging problems related to protein therapeutics research and development.