Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Charge remote fragmentation in electron capture and electron transfer dissociation

Tools
- Tools
+ Tools

Li, Xiaojuan, Lin, Cheng, Han, L. (Liang), Costello, Catherine E. and O'Connor, Peter B. (2010) Charge remote fragmentation in electron capture and electron transfer dissociation. Journal of The American Society for Mass Spectrometry, Vol.21 (No.4). pp. 646-656. doi:10.1016/j.jasms.2010.01.001

Research output not available from this repository, contact author.
Official URL: http://dx.doi.org/10.1016/j.jasms.2010.01.001

Request Changes to record.

Abstract

Secondary fragmentations of three synthetic peptides (human alpha A crystallin peptide 1-11, the deamidated form of human beta B2 crystallin peptide 4-14, and amyloid beta peptide 25-35) were studied in both electron capture dissociation (ECD) and electron-transfer dissociation (ETD) mode. In ECD, in addition to c and z. ion formations, charge remote fragmentations (CRF) of z. ions were abundant, resulting in internal fragment formation or partial/entire side-chain losses from amino acids, sometimes several residues away from the backbone cleavage site, and to some extent multiple side-chain losses. The internal fragments were observed in peptides with basic residues located in the middle of the sequences, which was different from most tryptic peptides with basic residues located at the C-terminus. These secondary cleavages were initiated by hydrogen abstraction at the alpha-, beta-, or gamma-position of the amino acid side chain. In comparison, ETD generates fewer CRF fragments than ECD. This secondary cleavage study will facilitate ECD/ETD spectra interpretation, and help de novo sequencing and database searching. (J Am Soc Mass Spectrom 2010, 21, 646-656) (C) 2010 Published by Elsevier Inc. on behalf of American Society for Mass Spectrometry.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Q Science > QC Physics
Divisions: Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH): Dissociation, Tandem mass spectrometry, Amino acids, Charge transfer, Fragmentation reactions, Peptides -- Synthesis
Journal or Publication Title: Journal of The American Society for Mass Spectrometry
Publisher: Springer New York LLC
ISSN: 1044-0305
Official Date: April 2010
Dates:
DateEvent
April 2010Published
Volume: Vol.21
Number: No.4
Number of Pages: 11
Page Range: pp. 646-656
DOI: 10.1016/j.jasms.2010.01.001
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: National Institutes of Health (U.S.) (NIH), National Center for Research Resources (U.S.) (NCRR), National Heart, Lung, and Blood Institute (NHLBI), National Institute of General Medical Sciences (U.S.) (NIGMS), ACS Petroleum, Bruker Daltonics, MDS Sciex
Grant number: P41RR10888 (NIH/NCRR), N01HV28178 (NIH/NHLBI), R01GM078293 (NIH/NIGMS)

Data sourced from Thomson Reuters' Web of Knowledge

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item
twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us