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===Mass spectrometry=== [[Image:ThermoScientificOrbitrapElite.JPG|thumb|An Orbitrap [[mass spectrometer]] commonly used in proteomics]] {{main|Protein mass spectrometry|Mass spectrometry}} [[Mass spectrometry]] is one of the key methods to study the proteome.<ref>{{cite journal|last=Altelaar|first=AF|author2=Munoz, J |author3=Heck, AJ |title=Next-generation proteomics: towards an integrative view of proteome dynamics.|journal=Nature Reviews Genetics|date=January 2013|volume=14|issue=1|pages=35β48|pmid=23207911|doi=10.1038/nrg3356|s2cid=10248311}}</ref> Some important mass spectrometry methods include Orbitrap Mass Spectrometry, [[MALDI]] (Matrix Assisted Laser Desorption/Ionization), and [[Electrospray ionization|ESI (Electrospray Ionization).]] [[Peptide mass fingerprinting]] identifies a protein by cleaving it into short peptides and then deduces the protein's identity by matching the observed peptide masses against a [[sequence database]]. [[Tandem mass spectrometry]], on the other hand, can get sequence information from individual peptides by isolating them, colliding them with a non-reactive gas, and then cataloguing the fragment [[Ion (physics)|ion]]s produced.<ref>{{cite journal |title=Mass-Spectrometry-Based Draft of the Human Proteome |url=https://www.jpt.com/literature/Mass-Spectrometry-Based-Draft-of-the-Human-Proteome |journal=[[Nature (journal)|Nature]] |volume=509 |issue=7502 |pages=582β7 |bibcode=2014Natur.509..582W |last1=Wilhelm |first1=Mathias |last2=Schlegl |first2=Judith |last3=Hahne |first3=Hannes |last4=Gholami |first4=Amin Moghaddas |last5=Lieberenz |first5=Marcus |last6=Savitski |first6=Mikhail M. |last7=Ziegler |first7=Emanuel |last8=Butzmann |first8=Lars |last9=Gessulat |first9=Siegfried |last10=Marx |first10=Harald |last11=Mathieson |first11=Toby |last12=Lemeer |first12=Simone |last13=Schnatbaum |first13=Karsten |last14=Reimer |first14=Ulf |last15=Wenschuh |first15=Holger |last16=Mollenhauer |first16=Martin |last17=Slotta-Huspenina |first17=Julia |last18=Boese |first18=Joos-Hendrik |last19=Bantscheff |first19=Marcus |last20=Gerstmair |first20=Anja |last21=Faerber |first21=Franz |last22=Kuster |first22=Bernhard |year=2014 |doi=10.1038/nature13319 |pmid=24870543 |s2cid=4467721 |access-date=2016-09-29 |archive-date=2018-08-20 |archive-url=https://web.archive.org/web/20180820005653/https://www.jpt.com/literature/Mass-Spectrometry-Based-Draft-of-the-Human-Proteome |url-status=dead }}</ref> In May 2014, a draft map of the human proteome was published in ''[[Nature (journal)|Nature]]''.<ref>{{cite journal|last1=Kim|first1=Min-Sik|title=A draft map of the human proteome|journal=Nature|volume=509|doi=10.1038/nature13302|pmid=24870542|issue=7502|date=May 2014|pages=575β81|display-authors=etal|pmc=4403737|bibcode=2014Natur.509..575K}}</ref> This map was generated using high-resolution Fourier-transform mass spectrometry. This study profiled 30 histologically normal human samples resulting in the identification of proteins coded by 17,294 genes. This accounts for around 84% of the total annotated protein-coding genes.
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