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Ultraviolet photodissociation enhances top‐down mass spectrometry as demonstrated on green fluorescent protein variants
Author(s) -
Dang Xibei,
Young Nicolas L.
Publication year - 2014
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.201400114
Subject(s) - photodissociation , electron transfer dissociation , ultraviolet , dissociation (chemistry) , fragmentation (computing) , mass spectrometry , proteomics , chemistry , fluorescence , green fluorescent protein , electron ionization , tandem mass spectrometry , ion , photochemistry , biology , chromatography , physics , biochemistry , gene , optoelectronics , optics , ecology , organic chemistry , ionization
Ultraviolet photodissociation ( UVPD ) is a compelling fragmentation technique with great potential to enhance proteomics generally and top‐down MS specifically. In this issue, Cannon et al. (Proteomics 2014, 14 , 1165–1173) use UVPD to perform top‐down MS on several sequence variants of green fluorescent protein and compare the results to CID , higher energy collision induced dissociation, and electron transfer dissociation. As compared to the other techniques UVPD produces a wider variety of fragment ion types that are relatively evenly distributed across the protein sequences. Overall, their results demonstrate enhanced sequence coverage and higher confidence in sequence assignment via UVPD MS . Based on these and other recent results UVPD is certain to become an increasingly widespread and valuable tool for top‐down proteomics.