Analytical chemistry studies and uses instruments and methods used to separate, identify, and quantify matter. In practice separation, identification or quantification may constitute the entire analysis or be combined with another method. Modern Analytical Chemistry is dominated by instrumental analysis. Many analytical chemists focus on a single type of instrument. Academics tend to either focus on new applications and discoveries or on new methods of analysis. Spectroscopy based on the differential interaction of the analyte along with electromagnetic radiation. Chromatography, in which the analyte is separated from the rest of the sample so that it may be measured without interference from other compounds.

The practice of Mass Spectrometry is one of the methods of Analytical Chemistry that has undergone the greatest change during the past 25 years. Mass spectrometry is the most significant and far reaching of these developments, allowing the generation of data in the Medical Sciences that brings new insights into critical questions. The role of mass spectrometry in genomics, proteomics, Metabolomics, Lipidomics and Future prospects for the Mass Spectrometry industry and Advances in mass spectrometry instrumentation and method are the Future developments in Mass Spectrometry

Mass spectrometry is an analytic technique with high specificity and a growing presence in laboratory medicine. Various types of Mass Spectrometers are being used in an increasing number of clinical laboratories around the world, and, as a result, significant improvements in assay performance are occurring rapidly in areas such as toxicology, endocrinology, and Biochemical genetics.

Imaging Mass Mpectrometry combines the chemical specificity and parallel detection of Mass Spectrometry with microscopic imaging capabilities. Imaging Mass Spectrometry is a technology that combines advanced analytical techniques for the analysis of Biomedical Chromatography with spatial fidelity. Imaging Mass Spectrometry is a technology that combines advanced analytical techniques for the analysis of Biomedical Chromatography with spatial fidelity. An effective approach for imaging biological specimens in this way utilizes Matrix-Assisted Laser Desorption Ionization Mass Spectrometry (MALDI MS)

High Performance Liquid Chromatography (HPLC) is a form of column chromatography that pumps a sample mixture or analyte in a solvent (known as the mobile phase) at high pressure through a column with Chromatographic packing material (stationary phase). The sample is carried by a moving carrier gas stream of helium or nitrogen. HPLC is used in a variety of industrial and scientific applications, such as Pharmaceutical, environmental, forensics, and chemicals.

            Main components in an HPLC system include the solvent reservoir, or multiple reservoirs, a high-pressure pump, a column, injector system and the detector.

Gas chromatography (GC) uses a gaseous mobile phase such as helium or hydrogen to push molecules through a column that serves as the stationary phase. The most common type of Mass Spectrometer (MS) associated with a Gas chromatography (GC) is the quadrupole Mass Spectrometer. GC is predominantly limited to volatile, heat-stable compounds lacking polar functional groups; however, chemical modification with derivatizing agents allows for functional groups to be masked, producing less polar, GC-compatible compounds. Gas Chromotography is the method most often used for comprehensive drug screening in the clinical laboratory using a combination of GC and Mass Spectrometry (GC-MS).

Tandem mass spectrometry, also known as MS/MS or MS2, involves multiple steps of Mass Spectrometry selection, with some form of fragmentation occurring in between the stages. In a Tandem mass spectrometer, ions are formed in the ion source and separated by mass-to-charge ratio in the first stage of Mass spectrometry. A common tandem Mass Spectrometry (MS/MS) analyzer will have 3 quadrupoles, denoted Q1, q2, and Q3. Q1 and Q3 are true Mass Analyzers using combinations of voltages and frequencies as described. There are various methods for fragmenting molecules for Tandem MS, including collision-induced dissociation (CID), electron capture dissociation (ECD), infrared multiphoton dissociation (IRMPD) and Blackbody Infrared Radiative Dissociation (BIRD)

There are several special techniques in chromatography that addresses key areas of distillation, physical sorption, absorption and heat exchange, and membranes. There are several techniques of chromatography. They are chromatographic bed shape which includes column chromatography, planar chromatography, paper chromatography, thin layer chromatography (TLC). The other techniques are by physical state of mobile phase which include gas chromatography and liquid chromatography. Another technique is by separation mechanism which includes ion exchange chromatography, expanded bed adsorption chromatographic, and size-exclusion chromatography. This session further discusses in detail about the techniques of chromatography.

High-resolution mass spectrometry (HRMS), which is used for residue analysis in food, has gained wider acceptance in the last few years. The main features of mass spectrometry combined with separation instruments are discussed in food-related analysis. A recent applications of mass spectrometry (MS)-based techniques for the analysis of compounds of food concern. Substances discussed are naturally occurring compounds in food products such as lipids, oligosaccharides, proteins, vitamins, flavonoids and related substances.

Mass Spectrometry in the clinical laboratory has focused on drugs of abuse confirmations, new-born screening, and steroid analysis. Clinical applications of Mass Spectrometry continue to expand, and Mass Spectrometry is now being used in almost all areas of laboratory medicine. Mass Spectrometry (MS) is an analytical technique for determining the structures of unknown molecules and “fingerprint” identifications of known molecules that are present in gases, liquids, and solids. Mass Spectrometry is unsurpassed in its combination of sensitivity, specificity, and speed. Fully computerized and reliable instruments have made possible the use of this powerful tool in Clinical medicine.

Mass spectrometry has become the most frequently employed technique in doping control analysis to identify prohibited compounds ever since their use has been banned by international federations. The application of modern and powerful Analytical instruments consisting of Liquid chromatographs (LCs), sophisticated atmospheric pressure ion sources, and sensitive Mass analysers has improved quality as well as speed of doping control analyses markedly during the last 5 years.

Mass Spectrometry are extensively used in drug discovery and development, including drug metabolism research. Mass Spectrometry plays in the discovery and development of new therapeutics by both the Pharmaceutical and the Biotechnology Industries. Mass Spectrometry is an essential tool in determining the molecular mass information of interest by ionizing chemical compounds to generate charged molecules or molecule fragments. The most common forms of ionization in small molecule research are electron ionization (EI), atmospheric pressure chemical ionization (APCI), and electrospray ionization (ESI). Mass spectrometry is widely used for analysis of impurities and degradation products due to its high sensitivity and selectivity.

Mass spectrometry (MS) is the most comprehensive and versatile tool in large-scale proteomics. Mass spectrometry has arguably become the core technology in proteomics. Protein mass spectrometry refers to the application of Mass spectrometry to the study of proteins. Mass Spectrometry is an important method for the accurate mass determination and characterization of Proteins, and a variety of methods and instrumentations have been developed for its many uses. Mass Spectrometry consist of three basic components: an ion source, a mass analyser, and an ion detector.

Mass spectrometry is used commonly in forensic laboratories for the confirmation of drugs and identification of ignitable liquids. Mass spectroscopy, also called mass spectrometry, is a scientific method that analyzes a sample of material to determine its molecular makeup. By ionizing a sample, a scientist can cause it to separate into its individual ions. Mass spectrometry has become a valuable tool in forensic science, where it can provide clues from the barest traces left by a suspect. Mass spectrometry is also useful in analyzing trace evidence.

Electrospray ionization mass spectrometry (ESI-MS) is a powerful tool for the end-group analysis of synthetic polymers. The ESI process is particularly soft, by which macromolecules can be subjected to mass spectrometric analysis without fragmentation and even loosely bound end-group functionalities may fully be retained in the ionized molecule. This favorable feature is exploited for the detailed study of the initiation process in radical polymerization, where the spectrum of radicals that add to monomer remains as an imprint in the final polymeric material.

Biochemical applications of Mass Spectrometry (MS) are important in the Pharmaceutical industry. They comprise compositional analyses of biomolecules, especially proteins, and methods that measure molecular functions such as ligand binding. Mass Spectrometry (MS) has emerged as a front-runner technique in pharmaceutical analysis, covering both qualitative and quantitative aspects. In fact, the area of use of MS is increasing at such an unprecedented rate that new applications are getting developed almost on daily basis. 

There are many types of Ionization methods are used in Mass Spectrometry methods. The classic methods that most chemists are familiar with are Electron Impact (EI) and Fast Atom Bombardment (FAB). These techniques are not used much with modern Mass Spectrometry except EI for environmental work using GC-MS. Mass spectrometers measure the mass-to-charge (m/z) ratios of gas phase ions.  Creating gas phase ions is the role of the Ionization Method.