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Enhanced Protein Characterization Through Selective Derivatization And Electrospray Ionization Tandem Mass Spectrometry
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Book Synopsis Enhanced Protein Characterization Through Selective Derivatization and Electrospray Ionization Tandem Mass Spectrometry by : Lisa Anne Vasicek
Download or read book Enhanced Protein Characterization Through Selective Derivatization and Electrospray Ionization Tandem Mass Spectrometry written by Lisa Anne Vasicek and published by . This book was released on 2011 with total page 338 pages. Available in PDF, EPUB and Kindle. Book excerpt: There continue to be great strides in the field of proteomics but as samples become more complex, the ability to increase sequence coverage and confidence in the identification becomes more important. Several methods of derivatization have been developed that can be used in combination with tandem mass spectrometry to identify and characterize proteins. Three types of activation, including infrared multiphoton dissociation, ultraviolet photodissociation, and electron transfer dissociation, are enhanced in this dissertation and compared to the conventional method of collisional induced dissociation (CID) to demonstrate the improved characterization of proteins. A free amine reactive phosphate group was synthesized and used to modify the N-terminus of digested peptides. This phosphate group absorbs at the IR wavelength of 10.6 [mu]m as well as the Vacuum-ultraviolet (VUV) due to an aromatic group allowing modified peptides to be dissociated by infrared multi-photon dissociation (IRMPD) or ultraviolet photodissociation (UVPD) whereas peptides without this chromophore are less responsive to IR or UV irradiation. The PD spectra for these modified peptides yield simplified MS/MS spectra due to the neutralization of all N-terminal product ions from the incorporation the negatively charged phosphate moiety. This is especially advantageous for UVPD due to the great number of product ions produced due to the higher energy deposition of the UV photons. The MS/MS spectra also produce higher sequence coverage in comparison to CID of the modified or unmodified peptides due to more informative fragmentation pathways generated upon PD from secondary dissociation and an increased ion trapping mass range. IRMPD is also implemented for the first time on an orbitrap mass spectrometer to achieve high resolution analysis of IR chromophore-derivatized samples as well as top-down analysis of unmodified proteins. High resolution/high mass accuracy analysis is extremely beneficial for characterization of complex samples due to the likelihood of false positives at lower resolutions/accuracies. For electron transfer dissociation, precursor ions in higher charge states undergo more exothermic electron transfer and thus minimize non-dissociative charge reduction. In this dissertation, cysteine side chains are alkylated with a fixed charge to deliberately increase the charge states of peptides and improve electron transfer dissociation. ETD can also be used to study protein structure by derivatizing the intact structure with a hydrazone reagent. A hydrazone bond will be preferentially cleaved during ETD facilitating the recognition of any modified residues through a distinguishing ETD fragmentation spectrum.
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.
Book Synopsis Protein Sequencing and Identification Using Tandem Mass Spectrometry by : Michael Kinter
Download or read book Protein Sequencing and Identification Using Tandem Mass Spectrometry written by Michael Kinter and published by John Wiley & Sons. This book was released on 2005-04-12 with total page 321 pages. Available in PDF, EPUB and Kindle. Book excerpt: How to design, execute, and interpret experiments for protein sequencing using mass spectrometry The rapid expansion of searchable protein and DNA databases in recent years has triggered an explosive growth in the application of mass spectrometry to protein sequencing. This timely and authoritative book provides professionals and scientists in biotechnology research with complete coverage of procedures for analyzing protein sequences by mass spectrometry, including step-by-step guidelines for sample preparation, analysis, and data interpretation. Michael Kinter and Nicholas Sherman present their own high-quality, laboratory-tested protocols for the analysis of a wide variety of samples, demonstrating how to carry out specific experiments and obtain fast, reliable results with a 99% success rate. Readers will get sufficient experimental detail to apply in their own laboratories, learn about the proper selection and operation of instruments, and gain essential insight into the fundamental principles of mass spectrometry and protein sequencing. Coverage includes: * Peptide fragmentation and interpretation of product ion spectra * Basic polyacrylamide gel electrophoresis * Preparation of protein digests for sequencing experiments * Mass spectrometric analysis using capillary liquid chromatography * Techniques for protein identification by database searches * Characterization of modified peptides using tandem mass spectrometry And much more
Book Synopsis Microcharacterization of Proteins by : Roland Kellner
Download or read book Microcharacterization of Proteins written by Roland Kellner and published by John Wiley & Sons. This book was released on 2008-09-26 with total page 346 pages. Available in PDF, EPUB and Kindle. Book excerpt: Proteomics - the analysis of the whole set of proteins and their functions in a cell - is based on the revolutionary developments which have been achieved in protein analysis during the last years. The number of finished genome projects is growing and in parallel there is a dramatically increasing need to identify the products of revealed genes. Acting on a micro level modern protein chemistry increases our understanding of biological events by elucidating the relevant structure-function relationships. The second edition of the successful title Microcharacterization of Proteins presents a current overview of modern protein analysis: From sample preparation to sequence analysis, mass spectrometry and bioinformatics it informs about the tools needed in protein research. This makes the book indispensable for everyone involved in proteomics!
Book Synopsis New Methods in Peptide Mapping for the Characterization of Proteins by : William S. Hancock
Download or read book New Methods in Peptide Mapping for the Characterization of Proteins written by William S. Hancock and published by CRC Press. This book was released on 1995-10-23 with total page 280 pages. Available in PDF, EPUB and Kindle. Book excerpt: This text is devoted to the characterization of recombinant DNA-derived proteins by peptide mapping. It describes new technological procedures including capillary electrophoresis, analysis of glycopeptides and the use of electrospray and matrix-assisted laser desorption mass spectrometry. The book presents practical procedures for preparing a protein sample, the enzyme digestion, choice of separation method and procedures for the structural analysis of the separated species. Many figures of peptide maps illustrate typical results. Tables of summary information about digestion, separation conditions, and analyses of important protein samples are also presented.
Book Synopsis Plant Systems Biology by : Sacha Baginsky
Download or read book Plant Systems Biology written by Sacha Baginsky and published by Springer Science & Business Media. This book was released on 2007-06-25 with total page 362 pages. Available in PDF, EPUB and Kindle. Book excerpt: This volume aims to provide a timely view of the state-of-the-art in systems biology. The editors take the opportunity to define systems biology as they and the contributing authors see it, and this will lay the groundwork for future studies. The volume is well-suited to both students and researchers interested in the methods of systems biology. Although the focus is on plant systems biology, the proposed material could be suitably applied to any organism.
Book Synopsis Large ([less Than Or Equal To] 112 KDa) Protein Characterization by Electrospray Ionization Fourier-transform Mass Spectrometry by : Neil Lindstrom Kelleher
Download or read book Large ([less Than Or Equal To] 112 KDa) Protein Characterization by Electrospray Ionization Fourier-transform Mass Spectrometry written by Neil Lindstrom Kelleher and published by . This book was released on 1997 with total page 252 pages. Available in PDF, EPUB and Kindle. Book excerpt:
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
Book Synopsis Fundamental Studies of Protein Ionization for Improved Analysis by Electrospray Ionization Mass Spectrometry and Related Methods by : Kevin A. Douglass
Download or read book Fundamental Studies of Protein Ionization for Improved Analysis by Electrospray Ionization Mass Spectrometry and Related Methods written by Kevin A. Douglass and published by . This book was released on 2014 with total page 190 pages. Available in PDF, EPUB and Kindle. Book excerpt: Mass spectrometry is an analytical technique in which a sample is converted to gas phase ions that are subsequently separated and detected. It offers great speed, selectivity, and sensitivity during analysis, characteristics which have enabled it to become a leading method for the study of proteins. The applications of MS for these biologically significant macromolecules range from accurately determining identity and sequence to shedding light on post-translational modifications and protein molecule interactions. As a first step towards analysis by MS, gas-phase protein ions must be formed. A common method for ionization is electrospray ionization, where a liquid sample including the protein is charged, nebulized, and evaporated, resulting in bare protein ions. Although ESI has been used in this way for over two decades, many aspects of the protein charging mechanism remain unclear. To address this problem, my research has focused on identifying the factors that determine the extent of protein multiple charging during ESI and improving the ionization of proteins by desorption electrospray ionization. DESI is a method similar to ESI, except that the sample is desorbed from a surface by the spray instead of being present in it from the onset. A simple model was developed that enables the accurate prediction of protein multiple charging observed during ESI-MS if the protein sequence is known. Furthermore, the enhancement of multiple charging that is observed upon the addition of certain organic reagents, a phenomenon known as supercharging, was investigated and a novel mechanism of protein supercharging was proposed. The difficulty in analyzing large proteins by DESI-MS was studied using an innovative approach where DESI was separated into its individual sub-processes and their individual contributions to the DESI process were evaluated. As a result, core limitations to the DESI-MS of large proteins were identified. The results of my cumulative research efforts should lead to the improved MS analysis of proteins by spray ionization methods, including ESI and DESI.
Book Synopsis Protein Phosphorylation Analysis by Electrospray Mass Spectrometry by : Wolf D. Lehmann
Download or read book Protein Phosphorylation Analysis by Electrospray Mass Spectrometry written by Wolf D. Lehmann and published by . This book was released on 2010 with total page 379 pages. Available in PDF, EPUB and Kindle. Book excerpt: Written by an experienced and well-published individual, this unique reference source takes a forward-looking approach. It describes the concepts and practice of protein phosphorylation analysis by tanden mass spectrometry and related techniques. These include purification, enrichment, database searching, other software tools, synthesis, phosphatase treatment, phospho-specific staining methods, isoelectric focusing and element mass spectrometry. The book then goes on to cover the fragmentation behaviour of phosphopeptides in tandem MS (pos+neg ions) and the implementation of the particular features into an analytical strategy. Protein Phosphorylation Analysis by Electrospray Mass Spectrometry: A Guide to Concepts and Practice ends with a summary and discussion of useful internet and software tools currently available.
Book Synopsis Protein and Peptide Mass Spectrometry in Drug Discovery by : Michael L. Gross
Download or read book Protein and Peptide Mass Spectrometry in Drug Discovery written by Michael L. Gross and published by John Wiley & Sons. This book was released on 2011-09-26 with total page 484 pages. Available in PDF, EPUB and Kindle. Book excerpt: The book that highlights mass spectrometry and its application in characterizing proteins and peptides in drug discovery An instrumental analytical method for quantifying the mass and characterization of various samples from small molecules to large proteins, mass spectrometry (MS) has become one of the most widely used techniques for studying proteins and peptides over the last decade. Bringing together the work of experts in academia and industry, Protein and Peptide Mass Spectrometry in Drug Discovery highlights current analytical approaches, industry practices, and modern strategies for the characterization of both peptides and proteins in drug discovery. Illustrating the critical role MS technology plays in characterizing target proteins and protein products, the methods used, ion mobility, and the use of microwave radiation to speed proteolysis, the book also covers important emerging applications for neuroproteomics and antigenic peptides. Placing an emphasis on the pharmaceutical industry, the book stresses practice and applications, presenting real-world examples covering the most recent advances in mass spectrometry, and providing an invaluable resource for pharmaceutical scientists in industry and academia, analytical and bioanalytical chemists, and researchers in protein science and proteomics.
Book Synopsis Multistage Tandem Mass Spectrometry Strategies for the Targeted Analysis of Oxidative Protein Modifications by : Jennifer M. Froelich
Download or read book Multistage Tandem Mass Spectrometry Strategies for the Targeted Analysis of Oxidative Protein Modifications written by Jennifer M. Froelich and published by . This book was released on 2008 with total page 460 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Protein Mass Spectrometry by : Julian Whitelegge
Download or read book Protein Mass Spectrometry written by Julian Whitelegge and published by Elsevier. This book was released on 2008-10-09 with total page 563 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book is designed to be a central text for young graduate students interested in mass spectrometry as it relates to the study of protein structure and function as well as proteomics. It is a definite must-have work for:- libraries at academic institutions with Master and Graduate programs in biochemistry, molecular biology, structural biology and proteomics- individual laboratories with interests covering these areas - libraries and individual laboratories in the pharmaceutical and biotechnology industries. *Serves as an essential reference to those working in the field*Incorporates the contributions of prominent experts *Features comprehensive coverage and a logical structure
Book Synopsis Mass Spectrometry Analysis for Protein-Protein Interactions and Dynamics by : M. Chance
Download or read book Mass Spectrometry Analysis for Protein-Protein Interactions and Dynamics written by M. Chance and published by John Wiley & Sons. This book was released on 2008-09-22 with total page 325 pages. Available in PDF, EPUB and Kindle. Book excerpt: Presents a wide variety of mass spectrometry methods used to explore structural mechanisms, protein dynamics and interactions between proteins. Preliminary chapters cover mass spectrometry methods for examining proteins and are then followed by chapters devoted to presenting very practical, how-to methods in a detailed way. Includes footprinting and plistex specifically, setting this book apart from the competition.
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.
Book Synopsis Advancement of Photodissociation and Electron-based Tandem Mass Spectrometry Methods for Proteome Analysis by : James Andrew Madsen
Download or read book Advancement of Photodissociation and Electron-based Tandem Mass Spectrometry Methods for Proteome Analysis written by James Andrew Madsen and published by . This book was released on 2011 with total page 378 pages. Available in PDF, EPUB and Kindle. Book excerpt: The number and types of diagnostic ions obtained by infrared multiphoton dissociation (IRMPD) and collision induced dissociation (CID) were evaluated for supercharged peptide ions created by electrospray ionization of solutions spiked with mnitrobenzyl alcohol. IRMPD of supercharged peptide ions increased the sequence coverage compared to that obtained by CID for all charge states investigated. Multiply charged, N-terminally derivatized peptides were subjected to electron transfer reactions to produce singly charged, radical species. Upon subsequent "soft" CID, highly abundant z-type ions were formed nearly exclusively, which yielded simplified fragmentation patterns amenable to de novo sequencing methods. Furthermore, the simplified series of z ions were shown to retain labile phosphoric acid moieties. Infrared multiphoton dissociation (IRMPD) was implemented in a novel dual pressure linear ion trap for rapid "top-down" proteomics. Due to secondary dissociation, IRMPD yielded product ions in significantly lower charge states as compared to CID, thus facilitating more accurate mass identification and streamlining product ion assignment. This outcome was especially useful for database searching of larger proteins (~29 kDa) as IRMPD substantially improved protein identification and scoring confidence. Also, IRMPD showed an increased selectivity towards backbone cleavages N-terminal to proline and C-terminal to acidic residues (especially for the lowest precursor charge states). Ultraviolet photodissociation (UVPD) at 193 nm was implemented on a linear ion trap mass spectrometer for high-throughput proteomic workflows. Upon irradiation by a single 5 ns laser pulse, efficient photodissociation of tryptic peptides was achieved with production of a, b, c, x, y, and z sequence ions, in addition to immonium ions and v and w side-chain loss ions. The factors that influence the UVPD mass spectra and subsequent in silico database searching via SEQUEST were evaluated. 193 nm ultraviolet photodissociation (UVPD) was employed to sequence singly and multiply charged peptide anions. Upon dissociation by this method, a-/x-type, followed by d and w side-chain loss ions, were the most prolific and abundant sequence ions, often yielding 100% sequence coverage. LC-MS/UVPD analysis using high pH mobile phases yielded efficient characterization of acidic peptides from mitogen-activated protein kinases.
Book Synopsis Mass Spectrometry in Sports Drug Testing by : Mario Thevis
Download or read book Mass Spectrometry in Sports Drug Testing written by Mario Thevis and published by John Wiley & Sons. This book was released on 2010-12-13 with total page 294 pages. Available in PDF, EPUB and Kindle. Book excerpt: Enables you to detect, identify, and characterize hundreds of drugs that may be used by athletes Mass spectrometry has become essential to sports drug testing. This book examines both the principles of sports drug testing and the use of mass spectrometry techniques and mass spectral data to detect, identify, and characterize hundreds of known and unknown drugs that athletes may use to enhance their performance. The author provides a detailed overview of the mass spectrometry of numerous classes of therapeutics and agents, various analyzers to detect low- and high-molecular weight drugs, as well as techniques to discriminate between endogenously produced and synthetically derived compounds. Mass Spectrometry in Sports Drug Testing begins with a full chapter dedicated to the history of sports drug testing. Next, the book provides the principles and techniques needed to maximize the specificity and sensitivity of mass spectrometric assays, including: Detailed, step-by-step assays with sample preparation Discussion of both chromatographic separation and mass spectrometric analysis Characterization of analytes in order to unequivocally identify banned substances Mass spectrometric behavior of low- and high-molecular weight analytes Throughout the book, descriptive examples illustrate the principles, advantages, and limitations of different assays. Mass Spectrometry in Sports Drug Testing not only sets forth the role mass spectrometry plays in detecting drug use among athletes, it also adds new insights into the health and ethical issues of doping in sports.
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