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Tandem Mass Spectrometer Animation I CSIR NET Life Science I GATE Life Science I DBT JRF
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tandem mass spectrometry is a powerful method for analyzing and identifying peptides and proteins some proteins can be identified by comparing their mass to a database of known proteins in other cases all or part of the amino acid sequence must be determined before a protein can be identified when a protein is large the ability to uniquely identify it with a single mass measurement becomes more difficult to make this easier one can break down the peptide into smaller components all methods of mass spectrometry can determine a protein's mass however tandem mass spectrometry can also rapidly and accurately determine both the mass and amino acid sequence of a protein all mass spectrometers consist of three essential components the ion source the mass analyzer and the detector as its name suggests tandem mass spectrometry utilizes two spectrometers arranged in tandem the two spectrometers are separated by a collision cell which contains an ionized inert gas such as helium or argon as with any mass spectrometer the first step is to convert the protein sample into gaseous ions for example flashing a prepared sample with a laser pulse excites and vaporizes some of the sample into a hot gas when the vaporized protein molecules collide with one another charges are transferred from one molecule to another and the gaseous protein molecules become ionized with tandem mass spectrometry these initial gaseous protein ions are called precursor ions applying an electrostatic field accelerates the precursor ions through the first mass spectrometer after the precursor ions have been analyzed by the first mass spectrometer they enter a collision cell which contains an inert gas such as helium or argon the inert gas atoms collide with and fragment the precursor ions into smaller peptide chains these new smaller fragments are called product ions the product ions then pass through the second mass spectrometer the fragmentation of precursor ions into product ions occurs in chemically predictable ways fragmentation is due to the disruption of individual peptide bonds the cleavage of a peptide bond breaks the original protein ion into two smaller peptide ions these two smaller product ions contain the amino acid sequences before and after the cleavage site in this example the disruption of a peptide bond cleaves a single amino acid residue from the amino terminus of the peptide the precursor peptide has an initial mass to charge ratio of about 621 following the cleavage of the terminal residue the mass to charge ratio is reduced to about 492 this change in the mass to charge ratio of 129 corresponds with the calculated mass to charge value of a glutamate residue in this way the tandem mass spectrometer can identify the terminal amino acid residue the collisions between the precursor ions and the inert gas atoms create a family of product ions each product ion represents a fragment of the original peptide with one or more amino acids removed from one end by comparing the mass to charge ratio of these various product ions the tandem mass spectrometer can determine the entire amino acid sequence of the original peptide for simplicity only the carboxyl terminal peptide fragments are shown the mass spectrum of the product ions formed by the fragmentation of this peptide shows five different peaks each peak corresponds to a different sized fragment the differences in the mass to charge ratio between the peaks can be used to identify specific amino acid residues in this way the mass spectrum of the product ions reveals the amino acid sequence of the original peptide you
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