共 7 条
Ultraviolet photodissociation enhances top-down mass spectrometry as demonstrated on green fluorescent protein variants
被引:7
作者:

Dang, Xibei
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Florida State Univ, Natl High Magnet Field Lab, Ion Cyclotron Resonance Program, Tallahassee, FL 32310 USA
Florida State Univ, Dept Chem & Biochem, Tallahassee, FL 32310 USA Florida State Univ, Natl High Magnet Field Lab, Ion Cyclotron Resonance Program, Tallahassee, FL 32310 USA

Young, Nicolas L.
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Florida State Univ, Natl High Magnet Field Lab, Ion Cyclotron Resonance Program, Tallahassee, FL 32310 USA Florida State Univ, Natl High Magnet Field Lab, Ion Cyclotron Resonance Program, Tallahassee, FL 32310 USA
机构:
[1] Florida State Univ, Natl High Magnet Field Lab, Ion Cyclotron Resonance Program, Tallahassee, FL 32310 USA
[2] Florida State Univ, Dept Chem & Biochem, Tallahassee, FL 32310 USA
来源:
关键词:
Green fluorescent protein;
Technology;
Top-down proteomics;
Ultraviolet photodissociation;
NM;
D O I:
10.1002/pmic.201400114
中图分类号:
Q5 [生物化学];
学科分类号:
071010 ;
081704 ;
摘要:
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.
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页码:1128 / 1129
页数:2
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