Journal of The American Society for Mass Spectrometry

, Volume 28, Issue 9, pp 1823–1826 | Cite as

The Mechanism Behind Top-Down UVPD Experiments: Making Sense of Apparent Contradictions

Critical Insight
First Online:
Received:
Revised:
Accepted:

Abstract

Top-down ultraviolet photodissociation (UVPD) allows greater sequence coverage than any other currently available method, often fracturing the vast majority of peptide bonds in whole proteins. At the same time, UVPD can be used to dissociate noncovalent complexes assembled from multiple proteins without breaking any covalent bonds. Although the utility of these experiments is unquestioned, the mechanism underlying these seemingly contradictory results has been the subject of many discussions. Herein, some fundamental considerations of photochemistry are briefly summarized within the context of a proposed mechanism that rationalizes the experimental results obtained by UVPD. Considerations for future instrument design, in terms of wavelength choice and power, are briefly discussed.

Graphical Abstract

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Keywords

Top-down proteomics 266 nm 193 nm Direct dissociation Internal conversion 
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Notes

Acknowledgement

The NIH is thanked for financial support (National Institute of General Medical Sciences grant R01GM107099).

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Copyright information

© American Society for Mass Spectrometry 2017

Authors and Affiliations

  1. 1.Department of ChemistryUniversity of CaliforniaRiversideUSA

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