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      Electrospray Ionization Mass Spectrometry: A Technique to Access the Information beyond the Molecular Weight of the Analyte

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          Abstract

          The Electrospray Ionization (ESI) is a soft ionization technique extensively used for production of gas phase ions (without fragmentation) of thermally labile large supramolecules. In the present review we have described the development of Electrospray Ionization mass spectrometry (ESI-MS) during the last 25 years in the study of various properties of different types of biological molecules. There have been extensive studies on the mechanism of formation of charged gaseous species by the ESI. Several groups have investigated the origin and implications of the multiple charge states of proteins observed in the ESI-mass spectra of the proteins. The charged analytes produced by ESI can be fragmented by activating them in the gas-phase, and thus tandem mass spectrometry has been developed, which provides very important insights on the structural properties of the molecule. The review will highlight recent developments and emerging directions in this fascinating area of research.

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          Electrospray ionization for mass spectrometry of large biomolecules

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            Proteomic analysis of post-translational modifications.

            Post-translational modifications modulate the activity of most eukaryote proteins. Analysis of these modifications presents formidable challenges but their determination generates indispensable insight into biological function. Strategies developed to characterize individual proteins are now systematically applied to protein populations. The combination of function- or structure-based purification of modified 'subproteomes', such as phosphorylated proteins or modified membrane proteins, with mass spectrometry is proving particularly successful. To map modification sites in molecular detail, novel mass spectrometric peptide sequencing and analysis technologies hold tremendous potential. Finally, stable isotope labeling strategies in combination with mass spectrometry have been applied successfully to study the dynamics of modifications.
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              Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry.

              Peptide sequence analysis using a combination of gas-phase ion/ion chemistry and tandem mass spectrometry (MS/MS) is demonstrated. Singly charged anthracene anions transfer an electron to multiply protonated peptides in a radio frequency quadrupole linear ion trap (QLT) and induce fragmentation of the peptide backbone along pathways that are analogous to those observed in electron capture dissociation. Modifications to the QLT that enable this ion/ion chemistry are presented, and automated acquisition of high-quality, single-scan electron transfer dissociation MS/MS spectra of phosphopeptides separated by nanoflow HPLC is described.
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                Author and article information

                Journal
                Int J Anal Chem
                Int J Anal Chem
                IJAC
                International Journal of Analytical Chemistry
                Hindawi Publishing Corporation
                1687-8760
                1687-8779
                2012
                15 December 2011
                : 2012
                : 282574
                Affiliations
                Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai 400005, India
                Author notes
                *Shyamalava Mazumdar: shyamal@ 123456tifr.res.in

                Academic Editor: Troy D. Wood

                Article
                10.1155/2012/282574
                3348530
                22611397
                119e8a0c-1331-4c23-afdd-1f857eb27512
                Copyright © 2012 S. Banerjee and S. Mazumdar.

                This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 9 August 2011
                : 23 October 2011
                : 9 November 2011
                Categories
                Review Article

                Analytical chemistry
                Analytical chemistry

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