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Cleavage N-terminal to proline: analysis of a database of peptide tandem mass spectra

Academic Article
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Overview

authors

  • Breci, L. A.
  • Tabb, D. L.
  • Yates III, John
  • Wysocki, V. H.

publication date

  • May 2003

journal

  • Analytical Chemistry  Journal

abstract

  • Fragmentation at the Xxx-Pro bond was analyzed for a group of peptide mass spectra that were acquired in a Finnigan ion trap mass spectrometer and were generated from proteins digested by enzymes and identified by the Sequest algorithm. Cleavage with formation of a + b + y ions occurred more readily at the Xxx-Pro bond than at other locations in these peptides, and the importance of this cleavage varied by the identity of Xxx. The most abundant Xxx-Pro relative bond cleavage ratios were observed when Xxx was Val, His, Asp, Ile, and Leu, whereas the least abundant cleavage ratios occurred when Xxx was Gly or Pro. Rationalization for these cleavage ratios at Xxx-Pro may include contribution of the Asp or His side chain to enhanced cleavage or the conformation of Pro, Gly, and the aliphatic residues Val, Ile, and Leu at the Xxx location in the Xxx-Pro bond. Although unusual fragmentation behavior has been noted for Pro-containing peptides, this analysis suggests that fragmentation at the Xxx-Pro bond is predictable and that this information may be used to improve the identification of proteins if it is incorporated into peptide sequencing algorithms.

subject areas

  • Amino Acid Sequence
  • Gas Chromatography-Mass Spectrometry
  • Molecular Sequence Data
  • Peptides
  • Proline
  • Spectrometry, Mass, Electrospray Ionization
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Identity

International Standard Serial Number (ISSN)

  • 0003-2700

Digital Object Identifier (DOI)

  • 10.1021/ac026359i

PubMed ID

  • 12720328
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Additional Document Info

start page

  • 1963

end page

  • 1971

volume

  • 75

issue

  • 9

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