Mass spectrometry (MS) is an analytical technique that is used to measure the mass-to-charge ratio of ions. The results are presented as a mass spectrum, a plot of intensity as a function of the mass-to-charge ratio. Mass spectrometry is used in many different fields and is applied to pure samples as well as complex mixtures.
An ion source is a device that creates atomic and molecular ions. Ion sources are used to form ions for mass spectrometers, optical emission spectrometers, particle accelerators, ion implanters and ion engines.
A mass spectrum is a histogram plot of intensity vs. mass-to-charge ratio (m/z) in a chemical sample, usually acquired using an instrument called a mass spectrometer. Not all mass spectra of a given substance are the same; for example, some mass spectrometers break the analyte molecules into fragments; others observe the intact molecular masses with little fragmentation. A mass spectrum can represent many different types of information based on the type of mass spectrometer and the specific experiment applied. Common fragmentation processes for organic molecules are the McLafferty rearrangement and alpha cleavage. Straight chain alkanes and alkyl groups produce a typical series of peaks: 29 (CH3CH2+), 43 (CH3CH2CH2+), 57 (CH3CH2CH2CH2+), 71 (CH3CH2CH2CH2CH2+) etc.
Secondary-ion mass spectrometry (SIMS) is a technique used to analyze the composition of solid surfaces and thin films by sputtering the surface of the specimen with a focused primary ion beam and collecting and analyzing ejected secondary ions. The mass/charge ratios of these secondary ions are measured with a mass spectrometer to determine the elemental, isotopic, or molecular composition of the surface to a depth of 1 to 2 nm. Due to the large variation in ionization probabilities among elements sputtered from different materials, comparison against well-calibrated standards is necessary to achieve accurate quantitative results. SIMS is the most sensitive surface analysis technique, with elemental detection limits ranging from parts per million to parts per billion.
Tandem mass spectrometry, also known as MS/MS or MS2, is a technique in instrumental analysis where two or more stages of analysis using one or more mass analyzer are performed with an additional reaction step in between these analyses to increase their abilities to analyse chemical samples. A common use of tandem MS is the analysis of biomolecules, such as proteins and peptides.
In mass spectrometry, the quadrupole mass analyzer is a type of mass analyzer originally conceived by Nobel laureate Wolfgang Paul and his student Helmut Steinwedel. As the name implies, it consists of four cylindrical rods, set parallel to each other. In a quadrupole mass spectrometer (QMS) the quadrupole is the mass analyzer – the component of the instrument responsible for selecting sample ions based on their mass-to-charge ratio (m/z). Ions are separated in a quadrupole based on the stability of their trajectories in the oscillating electric fields that are applied to the rods.
In mass spectrometry, matrix-assisted laser desorption/ionization (MALDI) is an ionization technique that uses a laser energy-absorbing matrix to create ions from large molecules with minimal fragmentation. It has been applied to the analysis of biomolecules and various organic molecules, which tend to be fragile and fragment when ionized by more conventional ionization methods. It is similar in character to electrospray ionization (ESI) in that both techniques are relatively soft ways of obtaining ions of large molecules in the gas phase, though MALDI typically produces far fewer multi-charged ions.
Perylene or perilene is a polycyclic aromatic hydrocarbon with the chemical formula C20H12, occurring as a brown solid. It or its derivatives may be carcinogenic, and it is considered to be a hazardous pollutant. In cell membrane cytochemistry, perylene is used as a fluorescent lipid probe. It is the parent compound of a class of rylene dyes.
The mass-to-charge ratio (m/Q) is a physical quantity relating the mass (quantity of matter) and the electric charge of a given particle, expressed in units of kilograms per coulomb (kg/C). It is most widely used in the electrodynamics of charged particles, e.g. in electron optics and ion optics.
The history of mass spectrometry has its roots in physical and chemical studies regarding the nature of matter. The study of gas discharges in the mid 19th century led to the discovery of anode and cathode rays, which turned out to be positive ions and electrons. Improved capabilities in the separation of these positive ions enabled the discovery of stable isotopes of the elements. The first such discovery was with the element neon, which was shown by mass spectrometry to have at least two stable isotopes: 20Ne and 22Ne. Mass spectrometers were used in the Manhattan Project for the separation of isotopes of uranium necessary to create the atomic bomb.
In mass spectrometry, Orbitrap is an ion trap mass analyzer consisting of an outer barrel-like electrode and a coaxial inner spindle-like electrode that traps ions in an orbital motion around the spindle. The image current from the trapped ions is detected and converted to a mass spectrum using the Fourier transform of the frequency signal.
Electron-transfer dissociation (ETD) is a method of fragmenting multiply-charged gaseous macromolecules in a mass spectrometer between the stages of tandem mass spectrometry (MS/MS). Similar to electron-capture dissociation, ETD induces fragmentation of large, multiply-charged cations by transferring electrons to them. ETD is used extensively with polymers and biological molecules such as proteins and peptides for sequence analysis. Transferring an electron causes peptide backbone cleavage into c- and z-ions while leaving labile post translational modifications (PTM) intact. The technique only works well for higher charge state peptide or polymer ions (z>2). However, relative to collision-induced dissociation (CID), ETD is advantageous for the fragmentation of longer peptides or even entire proteins. This makes the technique important for top-down proteomics. The method was developed by Hunt and coworkers at the University of Virginia.
Time-of-flight mass spectrometry (TOFMS) is a method of mass spectrometry in which an ion's mass-to-charge ratio is determined by a time of flight measurement. Ions are accelerated by an electric field of known strength. This acceleration results in an ion having the same kinetic energy as any other ion that has the same charge. The velocity of the ion depends on the mass-to-charge ratio. The time that it subsequently takes for the ion to reach a detector at a known distance is measured. This time will depend on the velocity of the ion, and therefore is a measure of its mass-to-charge ratio. From this ratio and known experimental parameters, one can identify the ion.
Desorption atmospheric pressure photoionization (DAPPI) is an ambient ionization technique for mass spectrometry that uses hot solvent vapor for desorption in conjunction with photoionization. Ambient Ionization techniques allow for direct analysis of samples without pretreatment. The direct analysis technique, such as DAPPI, eliminates the extraction steps seen in most nontraditional samples. DAPPI can be used to analyze bulkier samples, such as, tablets, powders, resins, plants, and tissues. The first step of this technique utilizes a jet of hot solvent vapor. The hot jet thermally desorbs the sample from a surface. The vaporized sample is then ionized by the vacuum ultraviolet light and consequently sampled into a mass spectrometer. DAPPI can detect a range of both polar and non-polar compounds, but is most sensitive when analyzing neutral or non-polar compounds. This technique also offers a selective and soft ionization for highly conjugated compounds.
A hybrid mass spectrometer is a device for tandem mass spectrometry that consists of a combination of two or more m/z separation devices of different types.
In mass spectrometry, resolution is a measure of the ability to distinguish two peaks of slightly different mass-to-charge ratios ΔM, in a mass spectrum.
The Kendrick mass is defined by setting the mass of a chosen molecular fragment, typically CH2, to an integer value in amu (atomic mass units). It is different from the IUPAC definition, which is based on setting the mass of 12C isotope to exactly 12 amu. The Kendrick mass is often used to identify homologous compounds differing only by a number of base units in high resolution mass spectra. This definition of mass was first suggested in 1963 by chemist Edward Kendrick, and it has been adopted by scientists working in the area of high-resolution mass spectrometry, environmental analysis, proteomics, petroleomics, metabolomics, polymer analysis, etc.
Collision-induced dissociation (CID), also known as collisionally activated dissociation (CAD), is a mass spectrometry technique to induce fragmentation of selected ions in the gas phase. The selected ions are usually accelerated by applying an electrical potential to increase the ion kinetic energy and then allowed to collide with neutral molecules. In the collision, some of the kinetic energy is converted into internal energy which results in bond breakage and the fragmentation of the molecular ion into smaller fragments. These fragment ions can then be analyzed by tandem mass spectrometry.
John H. Beynon FRS was a Welsh chemist and physicist known for his work in mass spectrometry.
