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Infrared Spectroscopy of Fragments from Doubly Protonated Tryptic Peptides
Author(s) -
Bythell Benjamin J.,
Erlekam Undine,
Paizs Béla,
Maître Philippe
Publication year - 2009
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200800804
Subject(s) - protonation , oxazolone , chemistry , infrared spectroscopy , spectroscopy , tandem mass spectrometry , ion , mass spectrometry , peptide , diketopiperazines , computational chemistry , crystallography , analytical chemistry (journal) , stereochemistry , chromatography , organic chemistry , biochemistry , physics , quantum mechanics
Most proteins in proteomics are identified from tandem mass spectra of doubly protonated tryptic peptides. Statistical studies indicate that these spectra fall into two distinct classes. IR spectroscopy experiments and DFT calculations performed on model b 2 ions show that peptides producing Class I spectra form protonated oxazolone ions (see figure) and not protonated diketopiperazines as proposed elsewhere.