Abstract
Mass spectrometry is the method of choice for sequencing peptides and proteins and is the preferred choice for characterizing post-translational modifications (PTMs). The most commonly used dissociation method to characterize peptides (i.e. collision-induced dissociation (CID)), however, has some limitations when it comes to analyzing many PTMs. Because CID chemistry is influenced by amino acid side-chains, some modifications can alter or inhibit dissociation along the peptide backbone, thereby limiting sequence information and hindering identification of the modification site. Electron transfer dissociation (ETD) has emerged as an alternate dissociation technique that, in most cases, overcomes these limitations of CID because it is less affected by side chain chemistry. Here, we review recent applications of ETD for characterizing peptide and protein PTMs with a particular emphasis on the advantages of ETD over CID, the ways in which ETD and CID have been used in a complementary manner, and how peptide modifications can still influence ETD dissociation pathways.
Keywords: Collision-induced dissociation, glycosylation, oxidation, phosphorylation, post-translational modification, mass spectrometry, methylation, MS/MS, nitration, sulfation, collision-induced dissociation (CID), sequence information, hindering identification, Electron transfer dissociation, peptide modifications
Current Pharmaceutical Biotechnology
Title: Electron Transfer Dissociation of Modified Peptides and Proteins
Volume: 12 Issue: 10
Author(s): Yuping Zhou, Jia Dong and Richard W. Vachet
Affiliation:
Keywords: Collision-induced dissociation, glycosylation, oxidation, phosphorylation, post-translational modification, mass spectrometry, methylation, MS/MS, nitration, sulfation, collision-induced dissociation (CID), sequence information, hindering identification, Electron transfer dissociation, peptide modifications
Abstract: Mass spectrometry is the method of choice for sequencing peptides and proteins and is the preferred choice for characterizing post-translational modifications (PTMs). The most commonly used dissociation method to characterize peptides (i.e. collision-induced dissociation (CID)), however, has some limitations when it comes to analyzing many PTMs. Because CID chemistry is influenced by amino acid side-chains, some modifications can alter or inhibit dissociation along the peptide backbone, thereby limiting sequence information and hindering identification of the modification site. Electron transfer dissociation (ETD) has emerged as an alternate dissociation technique that, in most cases, overcomes these limitations of CID because it is less affected by side chain chemistry. Here, we review recent applications of ETD for characterizing peptide and protein PTMs with a particular emphasis on the advantages of ETD over CID, the ways in which ETD and CID have been used in a complementary manner, and how peptide modifications can still influence ETD dissociation pathways.
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Cite this article as:
Zhou Yuping, Dong Jia and W. Vachet Richard, Electron Transfer Dissociation of Modified Peptides and Proteins, Current Pharmaceutical Biotechnology 2011; 12 (10) . https://dx.doi.org/10.2174/138920111798357230
DOI https://dx.doi.org/10.2174/138920111798357230 |
Print ISSN 1389-2010 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4316 |
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