Encyclopedia of Spectroscopy and Spectrometry, Three-Volume Set
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Users can refer to an alphabetical article listing, or to a listing arranged according to subject area to locate articles. Further reading lists at the end of each article allow easy access to the primary literature. Extensive cross-referencing, a complete subject index, numerous figures, and color plates are included in each volume. Initial access to the online version offering extensive hypertext linking and advanced search tools is available to buyers of the print edition.
Ongoing access is maintained for a minimum annual fee. Show more Show less. The entries give short descriptions, references to classics in the field, and cross-references to other related techniques There are many professionals trained at an earlier time or learning new fields who would profit from this set in their libraries. There are many professionals A toroidal ion trap can be visualized as a linear quadrupole curved around and connected at the ends or as a cross section of a 3D ion trap rotated on edge to form the toroid, donut shaped trap.
The trap can store large volumes of ions by distributing them throughout the ring-like trap structure. This toroidal shaped trap is a configuration that allows the increased miniaturization of an ion trap mass analyzer. Additionally all ions are stored in the same trapping field and ejected together simplifying detection that can be complicated with array configurations due to variations in detector alignment and machining of the arrays.
As with the toroidal trap, linear traps and 3D quadrupole ion traps are the most commonly miniaturized mass analyzers due to their high sensitivity, tolerance for mTorr pressure, and capabilities for single analyzer tandem mass spectrometry e. Orbitrap instruments are similar to Fourier transform ion cyclotron resonance mass spectrometers see text below. Ions are electrostatically trapped in an orbit around a central, spindle shaped electrode. The electrode confines the ions so that they both orbit around the central electrode and oscillate back and forth along the central electrode's long axis.
This oscillation generates an image current in the detector plates which is recorded by the instrument. The frequencies of these image currents depend on the mass-to-charge ratios of the ions. Mass spectra are obtained by Fourier transformation of the recorded image currents. Orbitraps have a high mass accuracy, high sensitivity and a good dynamic range. Fourier transform mass spectrometry FTMS , or more precisely Fourier transform ion cyclotron resonance MS, measures mass by detecting the image current produced by ions cyclotroning in the presence of a magnetic field.
Detectors at fixed positions in space measure the electrical signal of ions which pass near them over time, producing a periodic signal. Since the frequency of an ion's cycling is determined by its mass-to-charge ratio, this can be deconvoluted by performing a Fourier transform on the signal. FTMS has the advantage of high sensitivity since each ion is "counted" more than once and much higher resolution and thus precision.
Ion cyclotron resonance ICR is an older mass analysis technique similar to FTMS except that ions are detected with a traditional detector. Ions trapped in a Penning trap are excited by an RF electric field until they impact the wall of the trap, where the detector is located. Ions of different mass are resolved according to impact time. The final element of the mass spectrometer is the detector. The detector records either the charge induced or the current produced when an ion passes by or hits a surface. Typically, some type of electron multiplier is used, though other detectors including Faraday cups and ion-to-photon detectors are also used.
Because the number of ions leaving the mass analyzer at a particular instant is typically quite small, considerable amplification is often necessary to get a signal. Microchannel plate detectors are commonly used in modern commercial instruments. No direct current is produced, only a weak AC image current is produced in a circuit between the electrodes.
Encyclopedia of Spectroscopy and Spectrometry, Three Volume Set from Cole-Parmer
Other inductive detectors have also been used. A tandem mass spectrometer is one capable of multiple rounds of mass spectrometry, usually separated by some form of molecule fragmentation. For example, one mass analyzer can isolate one peptide from many entering a mass spectrometer. A second mass analyzer then stabilizes the peptide ions while they collide with a gas, causing them to fragment by collision-induced dissociation CID. A third mass analyzer then sorts the fragments produced from the peptides.
Tandem MS can also be done in a single mass analyzer over time, as in a quadrupole ion trap. An important application using tandem mass spectrometry is in protein identification. Tandem mass spectrometry enables a variety of experimental sequences. Many commercial mass spectrometers are designed to expedite the execution of such routine sequences as selected reaction monitoring SRM and precursor ion scanning.
In SRM, the first analyzer allows only a single mass through and the second analyzer monitors for multiple user-defined fragment ions. SRM is most often used with scanning instruments where the second mass analysis event is duty cycle limited. These experiments are used to increase specificity of detection of known molecules, notably in pharmacokinetic studies.
Precursor ion scanning refers to monitoring for a specific loss from the precursor ion. This experiment is used to detect specific motifs within unknown molecules. Another type of tandem mass spectrometry used for radiocarbon dating is accelerator mass spectrometry AMS , which uses very high voltages, usually in the mega-volt range, to accelerate negative ions into a type of tandem mass spectrometer. When a specific combination of source, analyzer, and detector becomes conventional in practice, a compound acronym may arise to designate it succinctly.
Certain applications of mass spectrometry have developed monikers that although strictly speaking would seem to refer to a broad application, in practice have come instead to connote a specific or a limited number of instrument configurations. An example of this is isotope ratio mass spectrometry IRMS , which refers in practice to the use of a limited number of sector based mass analyzers; this name is used to refer to both the application and the instrument used for the application. An important enhancement to the mass resolving and mass determining capabilities of mass spectrometry is using it in tandem with chromatographic and other separation techniques.
In this technique, a gas chromatograph is used to separate different compounds. This stream of separated compounds is fed online into the ion source, a metallic filament to which voltage is applied. This filament emits electrons which ionize the compounds. The ions can then further fragment, yielding predictable patterns. Intact ions and fragments pass into the mass spectrometer's analyzer and are eventually detected. It differs from GC-MS in that the mobile phase is liquid, usually a mixture of water and organic solvents , instead of gas.
Most commonly, an electrospray ionization source is used in LC-MS.
Other popular and commercially available LC-MS ion sources are atmospheric pressure chemical ionization and atmospheric pressure photoionization. There are also some newly developed ionization techniques like laser spray. Capillary electrophoresis—mass spectrometry CE-MS is a technique that combines the liquid separation process of capillary electrophoresis with mass spectrometry.
The duty cycle of IMS the time over which the experiment takes place is longer than most mass spectrometric techniques, such that the mass spectrometer can sample along the course of the IMS separation. Mass spectrometry produces various types of data. The most common data representation is the mass spectrum.
Certain types of mass spectrometry data are best represented as a mass chromatogram. Other types of mass spectrometry data are well represented as a three-dimensional contour map. Mass spectrometry data analysis is specific to the type of experiment producing the data. General subdivisions of data are fundamental to understanding any data. Many mass spectrometers work in either negative ion mode or positive ion mode.
It is very important to know whether the observed ions are negatively or positively charged. This is often important in determining the neutral mass but it also indicates something about the nature of the molecules. Different types of ion source result in different arrays of fragments produced from the original molecules.
An electron ionization source produces many fragments and mostly single-charged 1- radicals odd number of electrons , whereas an electrospray source usually produces non-radical quasimolecular ions that are frequently multiply charged. Tandem mass spectrometry purposely produces fragment ions post-source and can drastically change the sort of data achieved by an experiment. Knowledge of the origin of a sample can provide insight into the component molecules of the sample and their fragmentations. A crudely prepared biological sample will probably contain a certain amount of salt, which may form adducts with the analyte molecules in certain analyses.
Sometimes samples are spiked with sodium or another ion-carrying species to produce adducts rather than a protonated species. Mass spectrometry can measure molar mass, molecular structure, and sample purity. Each of these questions requires a different experimental procedure; therefore, adequate definition of the experimental goal is a prerequisite for collecting the proper data and successfully interpreting it.
Since the precise structure or peptide sequence of a molecule is deciphered through the set of fragment masses, the interpretation of mass spectra requires combined use of various techniques. Usually the first strategy for identifying an unknown compound is to compare its experimental mass spectrum against a library of mass spectra.
0-12-226680-3 Encyclopedia of Spectroscopy and Spectrometry, Three Volume Set
If no matches result from the search, then manual interpretation  or software assisted interpretation of mass spectra must be performed. Computer simulation of ionization and fragmentation processes occurring in mass spectrometer is the primary tool for assigning structure or peptide sequence to a molecule. An a priori structural information is fragmented in silico and the resulting pattern is compared with observed spectrum.
Such simulation is often supported by a fragmentation library  that contains published patterns of known decomposition reactions. Software taking advantage of this idea has been developed for both small molecules and proteins. Analysis of mass spectra can also be spectra with accurate mass. A computer algorithm called formula generator calculates all molecular formulas that theoretically fit a given mass with specified tolerance. A recent technique for structure elucidation in mass spectrometry, called precursor ion fingerprinting , identifies individual pieces of structural information by conducting a search of the tandem spectra of the molecule under investigation against a library of the product-ion spectra of structurally characterized precursor ions.
Mass spectrometry has both qualitative and quantitative uses. These include identifying unknown compounds, determining the isotopic composition of elements in a molecule, and determining the structure of a compound by observing its fragmentation. Other uses include quantifying the amount of a compound in a sample or studying the fundamentals of gas phase ion chemistry the chemistry of ions and neutrals in a vacuum. MS is now commonly used in analytical laboratories that study physical, chemical, or biological properties of a great variety of compounds.
As an analytical technique it possesses distinct advantages such as: Increased sensitivity over most other analytical techniques because the analyzer, as a mass-charge filter, reduces background interference, Excellent specificity from characteristic fragmentation patterns to identify unknowns or confirm the presence of suspected compounds, Information about molecular weight, Information about the isotopic abundance of elements, Temporally resolved chemical data. A few of the disadvantages of the method is that it often fails to distinguish between optical and geometrical isomers and the positions of substituent in o-, m- and p- positions in an aromatic ring.
Also, its scope is limited in identifying hydrocarbons that produce similar fragmented ions. Mass spectrometry is also used to determine the isotopic composition of elements within a sample. Differences in mass among isotopes of an element are very small, and the less abundant isotopes of an element are typically very rare, so a very sensitive instrument is required. These instruments, sometimes referred to as isotope ratio mass spectrometers IR-MS , usually use a single magnet to bend a beam of ionized particles towards a series of Faraday cups which convert particle impacts to electric current.
A fast on-line analysis of deuterium content of water can be done using flowing afterglow mass spectrometry , FA-MS. Probably the most sensitive and accurate mass spectrometer for this purpose is the accelerator mass spectrometer AMS. Some isotope ratios are used to determine the age of materials for example as in carbon dating. Labeling with stable isotopes is also used for protein quantification. This method allows the study of gases as they evolve in solution.
This method has been extensively used for the study of the production of oxygen by Photosystem II. Several techniques use ions created in a dedicated ion source injected into a flow tube or a drift tube: selected ion flow tube SIFT-MS , and proton transfer reaction PTR-MS , are variants of chemical ionization dedicated for trace gas analysis of air, breath or liquid headspace using well defined reaction time allowing calculations of analyte concentrations from the known reaction kinetics without the need for internal standard or calibration.
An atom probe is an instrument that combines time-of-flight mass spectrometry and field-evaporation microscopy to map the location of individual atoms. Pharmacokinetics is often studied using mass spectrometry because of the complex nature of the matrix often blood or urine and the need for high sensitivity to observe low dose and long time point data.
The most common instrumentation used in this application is LC-MS with a triple quadrupole mass spectrometer. Tandem mass spectrometry is usually employed for added specificity. Standard curves and internal standards are used for quantitation of usually a single pharmaceutical in the samples. The samples represent different time points as a pharmaceutical is administered and then metabolized or cleared from the body.
Much attention is paid to the linearity of the standard curve; however it is not uncommon to use curve fitting with more complex functions such as quadratics since the response of most mass spectrometers is less than linear across large concentration ranges. There is currently considerable interest in the use of very high sensitivity mass spectrometry for microdosing studies, which are seen as a promising alternative to animal experimentation.
Mass spectrometry is an important method for the characterization and sequencing of proteins. In keeping with the performance and mass range of available mass spectrometers, two approaches are used for characterizing proteins. In the first, intact proteins are ionized by either of the two techniques described above, and then introduced to a mass analyzer. This approach is referred to as " top-down " strategy of protein analysis. The top-down approach however is largely limited to low-throughput single-protein studies.
In the second, proteins are enzymatically digested into smaller peptides using proteases such as trypsin or pepsin , either in solution or in gel after electrophoretic separation. Koppenaal is well-known for his fundamental science investigations and innovations in atomic mass spectrometry, including the initial development and demonstration of effective reaction cell technology and associated ion molecule reaction approaches for interference reduction in ICPMS. More recently he has developed and applied ultra-high resolution orbital trapping MS techniques to metallomics applications.
Reviews of the first edition: "There are many professionals. A good balance of both breadth and depth of coverage. Editors Lindon, Tranter, and Koppenaal are specialists in biological NMR spectroscopy, chiral analytical methods, and atomic mass spectrometry, respectively. This edition represents a major update; though the majority of entries are reprinted verbatim from the first edition CH, Dec'00, ; edited by Lindon, Tranter, and J. Holmes , the second edition features many new entries focused mainly on technologies that emerged in the last decade.
These include proteomics and NMR studies on biofluids. Clearly written and containing numerous figures some in full color , tables, and extensive references, entries are mostly understandable to a typical working chemist, though a minority are quite specialized. The alphabetical arrangement is usable, but a subject-based arrangement might be more convenient for researching related topics.
This encyclopedia is unique in its scope and depth.
- AMT - The airborne mass spectrometer AIMS – Part 1: AIMS-H2O for UTLS water vapor measurements.
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It aims to assemble a comprehensive, balanced collection of information about both established and cutting-edge spectroscopic and spectrometric science, covering theoretical and practical aspects while maintaining readability and accessibility. Inevitably, in such an ambitious work, some important topics in rapidly evolving fields will be overlooked; e.
Entries reprinted from the first edition were not updated at all. While newer entries often bring the information up-to-date, some of the older entries remain outdated, particularly in their bibliographies. Overall, this encyclopedia gathers vast amounts of information into a single work. Though imperfect, it is useful for working chemists and for others, including advanced students, as a reference in spectroscopy and spectrometry from ATR to Zeeman.
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