Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/4848
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Type: Journal article
Title: Negative ion fragmentations of deprotonated peptides: backbone cleavages directed through both Asp and Glu
Author: Brinkworth, C.
Dua, S.
Mc Anoy, A.
Bowie, J.
Citation: Rapid Communications in Mass Spectrometry, 2001; 15(20):1965-1973
Publisher: John Wiley & Sons Ltd
Issue Date: 2001
ISSN: 0951-4198
1097-0231
Statement of
Responsibility: 
Craig S. Brinkworth, Suresh Dua, Andrew M. McAnoy, John H. Bowie
Abstract: The collision-induced spectra of [M - H](-) ions of a variety of natural and synthetic amphibian peptides containing Asp and/or Glu exhibit characteristic gamma backbone cleavage ions that identify the positions of these residues in the peptide. A theoretical study suggests that the Glu cleavage involves an S(N)i reaction of the carboxylate anion from the Glu alpha side chain to form a deprotonated cyclic lactone. The presence of either Asp or Glu or other residues that effect pronounced side-chain cleavages (e.g. Ser or Thr) results in the normal alpha and beta backbone cleavages being reduced in comparison to those cleavages which originate from side chains.
Keywords: Animals; Anura; Ions; Aspartic Acid; Glutamic Acid; Peptides; Spectrometry, Mass, Fast Atom Bombardment; Amino Acid Sequence; Elementary Particle Interactions; Molecular Sequence Data; Mass Spectrometry
Description: The definitive version may be found at www.wiley.com
Provenance: Published Online: 1 Oct 2001
RMID: 0020010362
DOI: 10.1002/rcm.457
Published version: http://www3.interscience.wiley.com/cgi-bin/fulltext/85514010/PDFSTART
Appears in Collections:Chemistry publications

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