MASS SPECTROMETRY AND ITS APPLICATION IN PROTEOMICS

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GHAREHCHAHI J.; NAGHAVI M.R.; ALIZADEH H.

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Journal: MODERN GENETICS JOURNAL (MGJ) Year:2009 | Volume:3 | Issue:4 Page(s): 5-28

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Title

MASS SPECTROMETRY AND ITS APPLICATION IN PROTEOMICS

Author(s)

GHAREHCHAHI J. | NAGHAVI M.R. | ALIZADEH H. | Issue Writer Certificate

Keywords

MASS SPECTROMETRYQ3

PROTEOMICSQ2

PROTEIN IDENTIFICATION AND MASS ANALYZERQ3

Abstract

A mass spectrometer (MS) is an instrument that produces ions from analytes and separates them in the gas phase according to their mass-to-charge ratio (m/z). The technique has its origin from studies done by J. J. Thomson and his student F. W. Aston about the turn of the last century. Today MS is the most sensitive method for the structural characterization of biomolecules. Every mass spectrometer now consists of: an ion source, to produce ions from the sample; one or more mass analyzers, to separate the ions according to their m/z ratios; a detector, to register the number of ions emerging from the last analyser; and a computer, to process the data, to create the mass spectrum, and to control the instrument through feedback. Indeed MASS SPECTROMETRY analysis of peptides and proteins relies on soft ionization techniques that create intact gas-phase ions from biomolecules. The two soft ionization techniques that most commonly used for the mass spectrometric analysis of proteins and peptides are Electrospray ionization (ESI) and Matrix-assisted laser desorption ionisation (MALDI). There are two main routes by which proteins are identified using MS. The classical PROTEOMICS approach involves the separation of the proteins in a mixture by two dimensional gel electrophoresis (2DE), followed by in-gel tryptic digestion and peptide mass fingerprinting (PMF) by MALDI-TOF MS. In this approach, proteins are identified by comparison of the experimentally determined peptide masses with the predicted mass values of the peptides generated by a theoretical digestion of each protein in a database. Another approach involves the use of tandem MASS SPECTROMETRY (MS\MS) to obtain a short amino acid sequence (sequence tag) from protein, followed by database searching using sequence tag. Mass spectrometric methods can also be used to determine the type and site of post translational modifications (PTM) on single, purified protein.

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APA: Copy

GHAREHCHAHI, J., NAGHAVI, M.R., & ALIZADEH, H.. (2009). MASS SPECTROMETRY AND ITS APPLICATION IN PROTEOMICS. MODERN GENETICS JOURNAL (MGJ), 3(4), 5-28. SID. https://sid.ir/paper/116641/en

Vancouver: Copy

GHAREHCHAHI J., NAGHAVI M.R., ALIZADEH H.. MASS SPECTROMETRY AND ITS APPLICATION IN PROTEOMICS. MODERN GENETICS JOURNAL (MGJ)[Internet]. 2009;3(4):5-28. Available from: https://sid.ir/paper/116641/en

IEEE: Copy

J. GHAREHCHAHI, M.R. NAGHAVI, and H. ALIZADEH, “MASS SPECTROMETRY AND ITS APPLICATION IN PROTEOMICS,” MODERN GENETICS JOURNAL (MGJ), vol. 3, no. 4, pp. 5–28, 2009, [Online]. Available: https://sid.ir/paper/116641/en

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