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Enzyme‐cleavable tandem peptides for quantitative studies in MS ‐based proteomics
Author(s) -
Winter Dominic,
Hung ChienWen,
Jaskolla Thorsten W.,
Karas Michael,
Lehmann Wolf D.
Publication year - 2012
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.201200290
Subject(s) - peptide , chemistry , proteomics , bottom up proteomics , isobaric labeling , tandem mass spectrometry , proteolytic enzymes , cleavage (geology) , enzyme , chromatography , electrospray ionization , mass spectrometry , tandem mass tag , small molecule , peptide sequence , biochemistry , combinatorial chemistry , protein mass spectrometry , quantitative proteomics , biology , paleontology , fracture (geology) , gene
A novel type of peptide standard is introduced that consists of two peptides combined in one synthetic molecule and separated by a proteolytic cleavage site. Upon enzymatic digestion, the two peptides are released in a molar one‐to‐one ratio. This method enables the generation of exact equimolar mixtures of two peptides of any nature and origin, thereby providing a valuable tool for the investigation of fundamental phenomena in MS . The applicability of the method is exemplified by the analysis of the effect of peptide sequence variations on the relative ionization efficiency in ESI‐ and MALDI‐MS.