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Stability of Asp‐Pro bond under high and low energy collision induced dissociation conditions in the immunodominant epitope region of Herpes simplex virion glycoprotein D
Author(s) -
Mák M.,
Mezö G.,
Skribanek Zs.,
Hudecz F.
Publication year - 1998
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/(sici)1097-0231(19980715)12:13<837::aid-rcm248>3.0.co;2-z
Subject(s) - chemistry , fragmentation (computing) , electrospray ionization , peptide bond , mass spectrometry , collision induced dissociation , dissociation (chemistry) , peptide , fast atom bombardment , bond energy , ionization , crystallography , molecule , tandem mass spectrometry , ion , chromatography , organic chemistry , biochemistry , computer science , operating system
A series of truncated Herpes simplex virion peptides studied by fast atom bombardment mass spectrometry under high and low energy collision induced dissociation conditions showed preferential fragmentation of the aspartyl‐proline amide bond, compared to other peptide bonds. Electrospray ionization investigation proved that this favoured fragmentation can not be attributed to only the known proline effect, as a change from Asp to Asn in the peptide yielded an Asn‐Pro bond which was found to be stable under the same ionization conditions. This mass spectrometric behaviour is in good agreement with the observation that DP bonds are sensitive to acidic conditions. © 1998 John Wiley & Sons, Ltd.