Details the many benefits of applying mass spectrometry to supramolecular chemistry Except as a method for the most basic measurements, mass spectrometry (MS) has long been considered incompatible with supramolecular chemistry. Yet, with today's methods, the disconnect between these two fields is not warranted. Mass Spectrometry and Gas-Phase Chemistry of Non-Covalent Complexes provides a convincing look at how modern MS techniques offer supramolecular chemists a powerful investigatory toolset. Bringing the two fields together in an interdisciplinary manner, this reference details the many different topics associated with the study of non-covalent complexes in the gas phase. The text begins with brief introductions to supramolecular chemistry and such relevant mass spectrometric methods as ionization techniques, analyzers, and tandem MS experiments. The coverage continues with: How the analyte's transition into the gas phase changes covalent bonding How limitations and pitfalls in analytical methods may produce data misinterpretations Artificial supramolecular aggregates and their examination Biomolecules, their complexes, and their examination After the general remarks making up the first section of the book, the following sections describe specific experimental procedures and are illustrated with numerous examples and short tutorials. Detailed citations end each chapter. Mass spectrometrists, supramolecular chemists, students in these fields, and interested readers from other disciplines involving the study of non-covalent bonds will all value Mass Spectrometry and Gas-Phase Chemistry of Non-Covalent Complexes as an innovative and practical resource.

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.

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.

Describes and integrates the techniques of many advances in both chromatographic and mass spectrometric technologies. This book also covers various biophysical applications, such as H/D exchange for study of conformations, protein-protein and protein-metal and ligand interactions. It also describes atto-to-zepto-mole quantitation of 14C and 3H.

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 illustra

This volume explores the use of mass spectrometry for biomedical applications. Chapters focus on specific therapeutic areas such as oncology, infectious disease and psychiatry. Additional chapters focus on methodology as well as new technologies and instrumentation. This volume provides readers with a comprehensive and informative manual that will allow them to appreciate mass spectrometry and proteomic research but also to initiate and improve their own work. Thus the book acts as a technical guide but also a conceptual guide to the newest information in this exciting field. Mass spectrometry is the central tool used in proteomic research today and is rapidly becoming indispensable to the biomedical scientist. With the completion of the human genome project and the genomic revolution, the proteomic revolution has followed closely behind. Understanding the human proteome has become critical to basic and clinical biomedical research and holds the promise of providing comprehensive understanding of human physiological processes. In addition, proteomics and mass spectrometry are bringing unprecedented biomarker discovery and are helping to personalize medicine.

This monograph reviews all relevant technologies based on mass spectrometry that are used to study or screen biological interactions in general. Arranged in three parts, the text begins by reviewing techniques nowadays almost considered classical, such as affinity chromatography and ultrafiltration, as well as the latest techniques. The second part focusses on all MS-based methods for the study of interactions of proteins with all classes of biomolecules. Besides pull down-based approaches, this section also emphasizes the use of ion mobility MS, capture-compound approaches, chemical proteomics and interactomics. The third and final part discusses other important technologies frequently employed in interaction studies, such as biosensors and microarrays. For pharmaceutical, analytical, protein, environmental and biochemists, as well as those working in pharmaceutical and analytical laboratories.