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Protein Mass Spectrometry
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. Its applications include the identification of proteins and their post-translational modifications, the elucidation of protein complexes, their subunits and functional interactions, as well as the global measurement of proteins in proteomics. It can also be used to localize proteins to the various organelles, and determine the interactions between different proteins as well as with membrane lipids. The two primary methods used for the ionization of protein in mass spectrometry are electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI). These ionization techniques are used in conjunction with mass analyzers such as tandem mass spectrometry. In general, the prote ...
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Mass Spectrometer
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. A mass spectrum is a type of plot of the ion signal as a function of the mass-to-charge ratio. These spectra are used to determine the elemental or isotopic signature of a sample, the masses of particles and of molecules, and to elucidate the chemical identity or structure of molecules and other chemical compounds. In a typical MS procedure, a sample, which may be solid, liquid, or gaseous, is ionized, for example by bombarding it with a beam of electrons. This may cause some of the sample's molecules to break up into positively charged fragments or simply become positively charged without fragmenting. These ions (fragments) are then separated according ...
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Koichi Tanaka
is a Japanese electrical engineer who shared the Nobel Prize in Chemistry in 2002 for developing a novel method for mass spectrometric analyses of biological macromolecules with John Bennett Fenn and Kurt Wüthrich (the latter for work in NMR spectroscopy). Early life and education Tanaka was born and raised in Toyama, Japan, his biological mother died one month after he was born. Tanaka graduated from Tohoku University with a bachelor's degree in electrical engineering in 1983, afterward he joined Shimadzu Corporation, where he engaged in the development of mass spectrometers. Soft laser desorption For mass spectrometry analyses of a macromolecule, such as a protein, the analyte must be ionized and vaporized by laser irradiation. The problem is that the direct irradiation of an intense laser pulse on a macromolecule causes cleavage of the analyte into tiny fragments and the loss of its structure. In February 1985, Tanaka found that by using a mixture of ultra fine metal pow ...
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Quadrupole Ion Trap
A quadrupole ion trap or paul trap is a type of ion trap that uses dynamic electric fields to trap charged particles. They are also called radio frequency (RF) traps or Paul traps in honor of Wolfgang Paul, who invented the device and shared the Nobel Prize in Physics in 1989 for this work. It is used as a component of a mass spectrometer or a trapped ion quantum computer. Overview A charged particle, such as an atomic or molecular ion, feels a force from an electric field. It is not possible to create a static configuration of electric fields that traps the charged particle in all three directions (this restriction is known as Earnshaw's theorem). It is possible, however, to create an ''average'' confining force in all three directions by use of electric fields that change in time. To do so, the confining and anti-confining directions are switched at a rate faster than it takes the particle to escape the trap. The traps are also called "radio frequency" traps because the switc ...
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Peptide Mass Fingerprinting
Peptide mass fingerprinting (PMF) (also known as protein fingerprinting) is an analytical technique for protein identification in which the unknown protein of interest is first cleaved into smaller peptides, whose absolute masses can be accurately measured with a mass spectrometer such as MALDI-TOF or ESI-TOF. The method was developed in 1993 by several groups independently. The peptide masses are compared to either a database containing known protein sequences or even the genome. This is achieved by using computer programs that translate the known genome of the organism into proteins, then theoretically cut the proteins into peptides, and calculate the absolute masses of the peptides from each protein. They then compare the masses of the peptides of the unknown protein to the theoretical peptide masses of each protein encoded in the genome. The results are statistically analyzed to find the best match. The advantage of this method is that only the masses of the peptides have to be ...
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Mass Spectrometry
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. A mass spectrum is a type of plot of the ion signal as a function of the mass-to-charge ratio. These spectra are used to determine the elemental or isotopic signature of a sample, the masses of particles and of molecules, and to elucidate the chemical identity or structure of molecules and other chemical compounds. In a typical MS procedure, a sample, which may be solid, liquid, or gaseous, is ionized, for example by bombarding it with a beam of electrons. This may cause some of the sample's molecules to break up into positively charged fragments or simply become positively charged without fragmenting. These ions (fragments) are then separated accordin ...
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Fourier Transform Ion Cyclotron Resonance
Fourier-transform ion cyclotron resonance mass spectrometry is a type of mass analyzer (or mass spectrometer) for determining the mass-to-charge ratio (''m''/''z'') of ions based on the cyclotron frequency of the ions in a fixed magnetic field. The ions are trapped in a Penning trap (a magnetic field with electric trapping plates), where they are excited (at their resonant cyclotron frequencies) to a larger cyclotron radius by an oscillating electric field orthogonal to the magnetic field. After the excitation field is removed, the ions are rotating at their cyclotron frequency in phase (as a "packet" of ions). These ions induce a charge (detected as an image current) on a pair of electrodes as the packets of ions pass close to them. The resulting signal is called a free induction decay (FID), transient or interferogram that consists of a superposition of sine waves. The useful signal is extracted from this data by performing a Fourier transform to give a mass spectrum. History FT- ...
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Time-of-flight
Time of flight (ToF) is the measurement of the time taken by an object, particle or wave (be it acoustic, electromagnetic, etc.) to travel a distance through a medium. This information can then be used to measure velocity or path length, or as a way to learn about the particle or medium's properties (such as composition or flow rate). The traveling object may be detected directly (direct time of flight, dToF, e.g., via an ion detector in mass spectrometry) or indirectly (indirect time of flight, iToF, e.g., by light scattered from an object in laser doppler velocimetry). Overview In electronics, one of the earliest devices using the principle are ultrasonic distance-measuring devices, which emit an ultrasonic pulse and are able to measure the distance to a solid object based on the time taken for the wave to bounce back to the emitter. The ToF method is also used to estimate the electron mobility. Originally, it was designed for measurement of low-conductive thin films, later adjus ...
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Kurt Wüthrich
Kurt Wüthrich (born 4 October 1938 in Aarberg, Canton of Bern) is a Swiss chemist/biophysicist and Nobel Chemistry laureate, known for developing nuclear magnetic resonance (NMR) methods for studying biological macromolecules. Education and early life Born in Aarberg, Switzerland, Wüthrich was educated in chemistry, physics, and mathematics at the University of Bern before pursuing his PhD supervised by Silvio Fallab at the University of Basel, awarded in 1964. Career After his PhD, Wüthrich continued postdoctoral research with Fallab for a short time before leaving to work at the University of California, Berkeley for two years from 1965 with Robert E. Connick. That was followed by a stint working with Robert G. Shulman at the Bell Telephone Laboratories in Murray Hill, New Jersey from 1967 to 1969. Wüthrich returned to Switzerland, to Zürich, in 1969, where he began his career there at the ETH Zürich, rising to Professor of Biophysics by 1980. He currently maint ...
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Nobel Prize In Chemistry
) , image = Nobel Prize.png , alt = A golden medallion with an embossed image of a bearded man facing left in profile. To the left of the man is the text "ALFR•" then "NOBEL", and on the right, the text (smaller) "NAT•" then "MDCCCXXXIII" above, followed by (smaller) "OB•" then "MDCCCXCVI" below. , awarded_for = Outstanding contributions in chemistry , presenter = Royal Swedish Academy of Sciences , location = Stockholm, Sweden , reward = 9 million SEK (2017) , year = 1901 , holder = Carolyn R. Bertozzi, Morten P. Meldal and Karl Barry Sharpless (2022) , most_awards = Frederick Sanger and Karl Barry Sharpless (2) , website nobelprize.org, previous = 2021 , year2=2022, main=2022, next=2023 The Nobel Prize in Chemistry is awarded annually by the Royal Swedish Academy of Sciences to scientists in the various fields of chemistry. It is one of the five Nobel Prizes established by the will of Alfred Nobel in 1895, awarded for ...
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CRC Press
The CRC Press, LLC is an American publishing group that specializes in producing technical books. Many of their books relate to engineering, science and mathematics. Their scope also includes books on business, forensics and information technology. CRC Press is now a division of Taylor & Francis, itself a subsidiary of Informa. History The CRC Press was founded as the Chemical Rubber Company (CRC) in 1903 by brothers Arthur, Leo and Emanuel Friedman in Cleveland, Ohio, based on an earlier enterprise by Arthur, who had begun selling rubber laboratory aprons in 1900. The company gradually expanded to include sales of laboratory equipment to chemists. In 1913 the CRC offered a short (116-page) manual called the ''Rubber Handbook'' as an incentive for any purchase of a dozen aprons. Since then the ''Rubber Handbook'' has evolved into the CRC's flagship book, the '' CRC Handbook of Chemistry and Physics''. In 1964, Chemical Rubber decided to focus on its publishing ventures ...
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Journal Of Chemical Physics
''The Journal of Chemical Physics'' is a scientific journal published by the American Institute of Physics that carries research papers on chemical physics."About the Journal"
from the ''Journal of Chemical Physics'' website.
Two volumes, each of 24 issues, are published annually. It was established in 1933 when '''' editors refused to publish theoretical works. The editors have been: *2019-present: Tim Lian *2008–2018: *2007–2008:
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