Ultraviolet photodissociation enhances top-down mass spectrometry as demonstrated on green fluorescent protein variants.
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, XXXX-XXXX) 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.
Ion Cyclotron Resonance Program, National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL, USA; Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL, USA.
Xibei
X
Dang
Nicolas L
NL
Young
D049452:Green Fluorescent Proteins / Q000032:analysis* / Q000737:chemistry*; D040901:Proteomics / Q000379:methods*; D053719:Tandem Mass Spectrometry / Q000379:methods*
D049452:Green Fluorescent Proteins
Green fluorescent protein; Technology; Top-down proteomics; Ultraviolet photodissociation