Author: Christoph A. Schalley
Publisher: John Wiley & Sons
Release Date: 2009-09-08
Details the many benefits of applying mass spectrometry tosupramolecular chemistry Except as a method for the most basic measurements, massspectrometry (MS) has long been considered incompatible withsupramolecular chemistry. Yet, with today's methods, the disconnectbetween these two fields is not warranted. Mass Spectrometry andGas-Phase Chemistry of Non-Covalent Complexes provides aconvincing look at how modern MS techniques offer supramolecularchemists a powerful investigatory toolset. Bringing the two fields together in an interdisciplinary manner,this reference details the many different topics associated withthe study of non-covalent complexes in the gas phase. The textbegins with brief introductions to supramolecular chemistry andsuch relevant mass spectrometric methods as ionization techniques,analyzers, and tandem MS experiments. The coverage continueswith: How the analyte's transition into the gas phase changes covalentbonding How limitations and pitfalls in analytical methods may producedata misinterpretations Artificial supramolecular aggregates and their examination Biomolecules, their complexes, and their examination After the general remarks making up the first section of thebook, the following sections describe specific experimentalprocedures and are illustrated with numerous examples and shorttutorials. Detailed citations end each chapter. Massspectrometrists, supramolecular chemists, students in these fields,and interested readers from other disciplines involving the studyof non-covalent bonds will all value Mass Spectrometry andGas-Phase Chemistry of Non-Covalent Complexes as an innovativeand practical resource.
Author: Edmond de Hoffmann
Publisher: John Wiley & Sons
Release Date: 2007-10-29
The latest edition of a highly successful textbook, Mass Spectrometry, Third Edition provides students with a complete overview of the principles, theories and key applications of modern mass spectrometry. All instrumental aspects of mass spectrometry are clearly and concisely described: sources, analysers and detectors. Tandem mass spectrometry is introduced early on and then developed in more detail in a later chapter. Emphasis is placed throughout the text on optimal utilisation conditions. Various fragmentation patterns are described together with analytical information that derives from the mass spectra. This new edition has been thoroughly revised and updated and has been redesigned to give the book a more contemporary look. As with previous editions it contains numerous examples, references and a series of exercises of increasing difficulty to encourage student understanding. Updates include: Increased coverage of MALDI and ESI, more detailed description of time of flight spectrometers, new material on isotope ratio mass spectrometry, and an expanded range of applications. Mass Spectrometry, Third Edition is an invaluable resource for all undergraduate and postgraduate students using this technique in departments of chemistry, biochemistry, medicine, pharmacology, agriculture, material science and food science. It is also of interest for researchers looking for an overview of the latest techniques and developments.
Spectroscopy and Modeling of Biomolecular Building Blocks presents an overview of recent advances in the intertwining of the following research fields: photon and electron spectroscopy, quantum chemistry, modelling and mass-spectrometry. The coupling of these disciplines offers a new point of view to the understanding of isolated elementary building blocks of biomolecules and their assemblies. It allows the unambiguous separation between intrinsic properties of biomolecular systems and those induced by the presence of their environment. The first chapters provide background in modelling (I), frequency-resolved spectroscopy using microwave, infrared and UV photons, time-resolved spectroscopy in the femtosecond domain and energy-resolved electron spectroscopy (II) and production of gas-phase neutral and ionic biomolecular species, mass-spectrometry, ion mobility and BIRD techniques (III). Chapter IV is devoted to case studies of gas-phase experimental investigations coupled to quantum or classical calculations. The topics are structural studies of nucleobases and oligonucleotides, peptides and proteins, sugars; neuromolecules; non-covalent complexes; chiral systems, interactions of low-energy electrons with biomolecules in the radiation chemistry context and very large gas-phase biomolecular systems. The fifth chapter concerns the link between gas-phase and liquid-phase. Different treatments of solvation are illustrated through examples pointing out the influence of progressive addition of water molecules upon properties of nucleobases, peptides, sugars and neuromolecules. Offer a new perspective to the understanding of isolated elementary building blocks of bio molecules Includes case studies of experimental investigations coupled to quantum or classical calculations
Author: Joseph H. Banoub
Publisher: CRC Press
Release Date: 2009-12-21
Assembling the work of an international panel of researchers, Mass Spectrometry of Nucleosides and Nucleic Acids summarizes and reviews the latest developments in the field and provides a window on the next generation of analysis. Beginning with an overview of recent developments, the book highlights the most popular ionization methods and illustrates the diversity of strategies employed in the characterization and sequencing of DNA and RNA oligomers, nucleosides, nucleotides, and adducts. It describes studies performed on deoxyinosine and its analogues and provides an introduction to tandem mass spectrometry (MS/MS). Next, the contributors examine mass spectrometric application in the study of cyclic nucleotides in biochemical signal transduction. They analyze urinary modified nucleosides and explore DNA adducts. They discuss isotope labeling of DNA-mass spectrometry (ILD-MS) and examine various uses of electrospray ionization mass spectrometry (ESI-MS). The book reviews recent progress in the direct MS characterization of noncovalent nucleic acid-protein complexes, explores the interaction and ionization of guanidine-derived compounds with highly acidic biomolecules, and examines quantitative identification of nucleic acids via signature digestion products detected using mass spectrometry. The book describes a direct-infusion ESI-MS approach that can serve as a screening technique for the presence of modified nucleosides from small RNAs. Lastly, it discusses the LC-MS/MS method for the in vitro replication studies on damage-containing DNA substrates, and concludes with an examination of the influence of metal ions on the structure and reactivity of nucleic acids. The exciting developments in mass spectrometry technology have fueled incredible advances in our understanding of nucleic acids and their complexes. The contributions presented in this volume capture the range of these advances, helping to inspire new findings and avenues of research.
This volume describes and integrates the techniques and fundamentals of more than a decade of revolutionary advances in both chromatographic and mass spectrometric technologies that have enabled the direct investigation of biomacromolecules per se and have provided the analytical power base to usher in the new fields of proteomics and systems biology. It also covers new biophysical applications such as H/D exchange for study of conformations, protein-protein and protein-metal and ligand interactions. Finally it describes atto-to-zepto-mole quantitation of 14C and 3H by accelerator mass spectrometry. *Part 1 of 2 volumes about Mass Spectrometry *Authoritative and comprehensive treatment of protein mass spectrometry in human cell biology *Presents fundamentals, techniques, instrumentation and bioinformatics *Provides an overview of proteomics, protein-protein and protein-ligand binding, and biophysical studies
Author: W. Ens
Publisher: Springer Science & Business Media
Release Date: 2013-03-09
A NATO Advanced Research Workshop entitled New Methods for the Study of Molecular Aggregates was held at Tbe Lodge at Kananaskis Village, Alberta, Canada from 16 -20 June 1996. In fact the meeting was entirely concerned with the problem of analyzing biomolecular complexes, so the title of these proceedings has been altered to give a more precise description of the content. Tbe workshop was hosted by the time-of-flight group of the Department of Physics at the University of Manitoba, and was attended by 64 participants from around the world. '!\venty-one invited talks were given and 27 papers were presented as posters. Of the 48 contributions, 22 papers (12 orals, 10 posters) are included in these proceedings. Tbe subject of the conference was the investigation of noncovalent biomolecular complexes, with particular focus on the application of mass spectrometry to their characterization. '!\vo new ionization techniques introduced in the late 1980s, electrospray ionization (ES I) and matrix-assisted laser desorptionlionization (MALDI), resulted in a breakthrough in mass spectrometry, enabling its use in molecular weight and primary structure determination of biopolymers larger than 100 kDa. Recently it has been discovered that ESI mass spectrometry mayaiso be used to characterize complexes containing noncovalent interactions, thus opening new perspectives for supramolecular chemistry. ESI mass spectrometry has the advantage that the sampie is introduced from a homogenous solution which can be maintained at near physiological conditions of pR, concentration, and temperature.
Author: Klaus Wanner
Publisher: John Wiley & Sons
Release Date: 2007-04-09
This first overview of mass spectrometry-based pharmaceutical analysis is the key to improved high-throughput drug screening, rational drug design and analysis of multiple ligand-target interactions. The ready reference opens with a general introduction to the use of mass spectrometry in pharmaceutical screening, followed by a detailed description of recently developed analytical systems for use in the pharmaceutical laboratory. Applications range from simple binding assays to complex screens of biological activity and systems containing multiple targets or ligands -- all highly relevant techniques in the early stages in drug discovery, from target characterization to hit and lead finding.
This dissertation focuses on coupling separation techniques such as ion mobility (IM) and liquid chromatography (LC) to mass spectrometry and their application to characterization of complex mixtures. Non-covalent complexes between poly(ethylene imine) (PEI) and single stranded oligodeoxynucleotides (ODNs), as well as components from black raspberries, were characterized utilizing ion mobility mass spectrometry (IM-MS) and liquid chromatography mass spectrometry (LC-MS), respectively. Interfacing these separation methods to mass spectrometry allows for detection and identification of isobaric species and species present in low concentration. Non-covalent complexes between low molecular weight poly(ethylene imine) (PEI 400 and 800) and single-stranded oligodeoxynucleotides (ODNs) were investigated for five ODNs, including d(TTTTT), d(CCCCC), d(AAAAA), d(GGGGG) and d(GCGAT). In chapter 4 the compositions, as well as solution and gas-phase stabilities of the complexes (termed polyplexes) were examined by electrospray ionization mass spectrometry (ESI-MS) and tandem mass spectrometry (MS2). Independent of the mixing ratio of the reactants, the polyplex with 1:1 polymer-to-nucleotide stoichiometry, PN, is the dominant product. The gas-phase stabilities, assessed by MS2 and collisionally activated dissociation, follow the same order, providing evidence that the polyplex structures in aqueous solution and the more hydrophobic environment of the gas phase are very similar. Non-covalent complexes with different composition but the same molecular mass were corroborated by ion mobility mass spectrometry (IM-MS). In chapter 5 of this dissertation an investigation of the expanded non-covalent system, ternary complexes, of poly(ethylene imine), single-stranded oligodeoxynucleotides and glutamic acid entities, is discussed. The solution stabilities and gas-phase stabilities of the ternary complexes (termed terplexes) were examined by electrospray ionization mass spectrometry (ESI-MS) and tandem mass spectrometry (MS2). In addition, higher order ternary structures with multiple units of polymer and/or nucleotide present within the terplex were identified utilizing IM-MS. Finally, chapter 6 provides information on characterization of non-anthocyanin components from black raspberry fractions by interfacing liquid chromatography (LC) to mass spectrometry. The black raspberry extracts were provided from the lab of Dr. Joseph C. Scheerens at Ohio Agricultural Research and Development Center, Wooster, Ohio. Combination of LC-MS, ESI-MS and MS2 provided structural information for the corresponding components.
Author: Roza Maria Kamp
Publisher: Springer Science & Business Media
Release Date: 2004-01-23
Following the succesful publication of "Proteome and Protein Analysis" in 2000, which was based on a former MPSA (Methods in Protein Structure Analysis) conference, "Methods in Proteome and Protein Analysis" presents the most interesting papers from the 14th MPSA meeting. Selected contributions discuss the latest techniques and approaches for analysing protein and proteome structures. Major topics include: protein and peptide sample preparation and separation new reagent for protein sequence analysis mass spectrometry in protein research analysis of posttranslational modification protein-protein interaction using MALDI-MS manipulation of genome or functional compositon trap structure-function correlation study using optical biosensors of microcolorimetrical techniques structural proteomics as NMR or fluorescence polarization study the classification and prediction of structure or functional sites in silico analysis of proteins and proteomes increasing throughput and data quality for proteomics
Author: Igor A. Kaltashov
Publisher: John Wiley & Sons
Release Date: 2012-03-02
The definitive guide to mass spectrometry techniques in biologyand biophysics The use of mass spectrometry (MS) to study the architecture anddynamics of proteins is increasingly common within the biophysicalcommunity, and Mass Spectrometry in Structural Biology andBiophysics: Architecture, Dynamics, and Interaction ofBiomolecules, Second Edition provides readers with detailed,systematic coverage of the current state of the art. Offering an unrivalled overview of modern MS-based armamentariumthat can be used to solve the most challenging problems inbiophysics, structural biology, and biopharmaceuticals, the book isa practical guide to understanding the role of MS techniques inbiophysical research. Designed to meet the needs of both academicand industrial researchers, it makes mass spectrometry accessibleto professionals in a range of fields, includingbiopharmaceuticals. This new edition has been significantly expanded and updated toinclude the most recent experimental methodologies and techniques,MS applications in biophysics and structural biology, methods forstudying higher order structure and dynamics of proteins, anexamination of other biopolymers and synthetic polymers, such asnucleic acids and oligosaccharides, and much more. Featuring high-quality illustrations that illuminate theconcepts described in the text, as well as extensive referencesthat enable the reader to pursue further study, Mass Spectrometryin Structural Biology and Biophysics is an indispensable resourcefor researchers and graduate students working in biophysics,structural biology, protein chemistry, and related fields.