Peptide and protein de novo sequencing by mass spectrometry
peer-reviewed · Current Opinion in Structural Biology · 2003
peer-reviewed · Current Opinion in Structural Biology · 2003. Kenneth G. Standing. Although the advent of large-scale genomic sequencing has greatly simplified the task of determining the…
| Date | 2003-10-01 |
| Type | peer-reviewed |
| Venue | Current Opinion in Structural Biology |
| Publisher | Elsevier BV |
| Contribution | review |
| DOI | 10.1016/j.sbi.2003.09.005 |
| Citations (OpenAlex) | 151 |
| Venue 2-year citedness | 8.41 |
Abstract
Although the advent of large-scale genomic sequencing has greatly simplified the task of determining the primary structures of peptides and proteins, the genomic sequences of many organisms are still unknown. Even for those that are known, modifications such as post-translational events may prevent the identification of all or part of the protein sequence. Thus, complete characterization of the protein primary structure often requires determination of the protein sequence by mass spectrometry with minimal assistance from genomic data - de novo protein sequencing. This task has been facilitated by technical developments during the past few years: ‘soft’ ionization techniques, new forms of chemical modification (derivatization), new types of mass spectrometer and improved software.
Methods and tools
- Peptide and protein de novo sequencing by mass spectrometry: Current Opinion in Structural Biology review on peptide and protein de novo sequencing by mass spectrometry.
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