Protein primary structure using orthogonal fragmentation techniques in Fourier transform mass spectrometry

Author: Zubarev, Roman

Source: Expert Review of Proteomics, Volume 3, Number 2, April 2006 , pp. 251-261(11)

Buy & download fulltext article:

Price: $73.00 plus tax (Refund Policy)

Abstract:

Proteomics analysis using tandem mass spectrometry requires informative backbone fragmentation of peptide ions. Collision-activated dissociation (CAD) of cations alone is not sufficiently informative to satisfy all requirements. Thus, there is a need to supplement CAD with a complementary fragmentation technique. Electron capture dissociation (ECD) is complementary to collisional excitation in terms of the cleavage of a different bond (N-C_α versus C-N bond) and other properties. CAD-ECD combination improves protein identification and enables high-throughput de novo sequencing of peptides. ECD and its variants are also useful in mapping labile post-translational modifications in proteins and isomer differentiation; for example, distinguishing Ile from Leu, iso-Asp from Asp and even D- from L-amino acid residues.

Keywords: collision–activated dissociation; electron capture dissociation; Fourier transform mass spectrometry; peptide fragmentation; post–translational modification; protein identification

Document Type: Research article

DOI: http://dx.doi.org/10.1586/14789450.3.2.251

Publication date: 2006-04-01

More about this publication?

Expert Review of Proteomics explores technologies, methods and discoveries from the field of proteomics to advance scientific understanding of the many varied roles protein expression plays in human health and disease.
Editorial Board
Information for Authors
Submit a Paper
Subscribe to this Title
Information for Advertisers
Terms & Conditions
Information for Librarians
Free Trials
ingentaconnect is not responsible for the content or availability of external websites