Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

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

Stability of Asp‐Pro bond under high and low energy collision induced dissociation conditions in... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Rapid Communications in Mass Spectrometry Wiley

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

Download PDF
6 pages

Loading next page...
 
/lp/wiley/stability-of-asp-pro-bond-under-high-and-low-energy-collision-induced-dw05sZDP4p

References (0)

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

Publisher
Wiley
Copyright
Copyright © 1998 Wiley Subscription Services
ISSN
0951-4198
eISSN
1097-0231
DOI
10.1002/(SICI)1097-0231(19980715)12:13<837::AID-RCM248>3.0.CO;2-Z
pmid
9684378
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Rapid Communications in Mass Spectrometry – Wiley

Published: Jan 15, 1998

There are no references for this article.