Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||Negative ion fragmentations of deprotonated peptides: backbone cleavages directed through both Asp and Glu|
Mc Anoy, A.
|Citation:||Rapid Communications in Mass Spectrometry, 2001; 15(20):1965-1973|
|Publisher:||John Wiley & Sons Ltd|
|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.|
Spectrometry, Mass, Fast Atom Bombardment
Amino Acid Sequence
Elementary Particle Interactions
Molecular Sequence Data
|Description:||The definitive version may be found at www.wiley.com|
|Provenance:||Published Online: 1 Oct 2001|
|Appears in Collections:||Aurora harvest 6|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.