Abstract
Peptides are sequenced using a magnetic sector tandem mass spectrometer by analyzing the product ions resulting from high-energy collisions between the peptide precursor ion and an inert gas (1). These collisions result in product ion spectra with features specific to high-energy collision-induced dissociation (CID). Ideally, the product ion pattern will be sufficient to sequence the peptide analyte. For some peptides, however, the fragmentation pattern will not be amenable to complete interpretation, and further measures must be taken to improve the results. One such measure that has been found to improve the interpretability of CID spectra is derivatization of the N-terminus of the peptide with a fixed-charge bearing group (2–4). Section 1.1. summarizes the salient features of the high-energy CID spectra of peptides and describes the rationale behind the best use of N-terminal charged derivatives. Several examples are shown in which charged derivatives improve the interpretability of CID spectra. Section 1.2. discusses synthetic schemes for attaching a charged group to a peptide N-terminus, and Sections 2. and 3. describe the synthesis of trimethylammoniumacetyl (TMAA)-peptide derivatives.
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© 1996 Humana Press Inc., Totowa, NJ
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Zaia, J. (1996). Charged Derivatives for Peptide Sequencing Using a Magnetic Sector Instrument. In: Chapman, J.R. (eds) Protein and Peptide Analysis by Mass Spectrometry. Methods in Molecular Biology™, vol 61. Humana Press. https://doi.org/10.1385/0-89603-345-7:29
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DOI: https://doi.org/10.1385/0-89603-345-7:29
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