Dissociation mechanisms and implication for the presence of multiple conformations for peptide ions with arginine at the C-terminus: time-resolved photodissociation study

Cited 14 time in scopus
Metadata Downloads
Title
Dissociation mechanisms and implication for the presence of multiple conformations for peptide ions with arginine at the C-terminus: time-resolved photodissociation study
Author(s)
S H Yoon; Jeong Hee Moon; M S Kim
Bibliographic Citation
Journal of Mass Spectrometry, vol. 45, no. 7, pp. 806-814
Publication Year
2010
Abstract
Time-resolved photodissociation (PD) patterns of singly protonated peptides with arginine at the C-terminus (C-arg peptide ions) have been used to classify the dissociation channels into two categories, i.e. high-energy channels generating v, w and x and low-energy ones generating b, y and z. x + 1 formed by Cα-CO cleavage seems to be the intermediate ion in high-energy channels just as a + 1 is for N-arg peptide ions. Difference in time-resolved pattern indicates that the two sets of channels, high- and low-energy ones, are not in direct competition. Noncompetitive dissociation is also indicated by the observation of anomalous effect of matrix used in matrix-assisted laser desorption ionization, a cooler matrix generating more high-energy product ions both in spontaneous dissociation and in PD. Results from detailed investigation suggest that the two sets of channels start from two (ormore) different conformations.
Keyword
Arginine at C-terminusConformationMatrix effectNoncompetitive dissociationPeptide ion dissociation mechanismPhotodissociationTandem TOFTime-resolved photodissociation
ISSN
1076-5174
Publisher
Wiley
DOI
http://dx.doi.org/10.1002/jms.1773
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.