Premium
C‐terminomics: Targeted analysis of natural and posttranslationally modified protein and peptide C‐termini
Author(s) -
Tanco Sebastian,
Gevaert Kris,
Damme Petra
Publication year - 2015
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201400301
Subject(s) - proteomics , computational biology , protein–protein interaction , biochemistry , biology , peptide , posttranslational modification , bottom up proteomics , chemistry , mass spectrometry , enzyme , tandem mass spectrometry , gene , protein mass spectrometry , chromatography
The C‐terminus (where C is carboxyl) of a protein can serve as a recognition signature for a variety of biological processes, including protein trafficking and protein complex formation. Hence, the identity of the in vivo protein C‐termini provides valuable information about biological processes. Analysis of protein C‐termini is also crucial for the study of C‐terminal PTMs, particularly for monitoring proteolytic processing by endopeptidases and carboxypeptidases. Although technical difficulties have limited the study of C‐termini, a range of technologies have been proposed in the last couple of years. Here, we review the current proteomics technologies for C‐terminal analysis, with a focus on the biological information that can be derived from C‐terminomics studies.