Protein primary structure using orthogonal fragmentation techniques in Fourier transform mass spectrometry
peer-reviewed · Expert Review of Proteomics · 2006
| Date | 2006-04-01 |
| Type | peer-reviewed |
| Venue | Expert Review of Proteomics |
| Publisher | Informa UK Limited |
| Contribution | review |
| DOI | 10.1586/14789450.3.2.251 |
| Citations (OpenAlex) | 44 |
| Venue 2-year citedness | 3.58 |
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-Calpha 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.
Methods and tools
- CAD-ECD orthogonal fragmentation review: Reviews how combining collision-activated dissociation with electron capture dissociation in Fourier transform MS gives complementary backbone cleavages that enable reliable high-throughput de novo peptide sequencing.