Infrared irradiation in the collision cell of a hybrid tandem quadrupole/time-of-flight mass spectrometer for declustering and cleaning of nanoelectrosprayed protein complex ions.
Herein we report the performance of a hybrid quadrupole time-of-flight tandem mass spectrometer with an improved designed for coaxial infrared laser introduction for the characterization and dissociation of large protein complex ions and their aggregates formed under nanoelectrospray ionization. The major improvement from the original design (Raspopov, S. A.; El-Faramawy, A.; Thomson, B. A.; Siu, K. W. M. Anal. Chem. 2006, 78, 4572-4577) involves the use of a hollow silica waveguide and physical isolation of the infrared laser. Large model protein complex ions and their aggregates examined include alcohol dehydrogenase, avidin, GroEL, and others. Gentle heating of these complexes with the infrared laser facilitated declustering and resulted in better resolved mass spectral peaks and more accurate molecular-weight measurements.
Centre for Research in Earth and Space Science, York University, 4700 Keele Street, Toronto, Ontario, Canada M3J 1P3.
Ayman
A
El-Faramawy
Yuzhu
Y
Guo
Udo H
UH
Verkerk
Bruce A
BA
Thomson
K W Michael
KW
Siu
D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D001360:Avidin / Q000737:chemistry*; D018834:Chaperonin 60 / Q000737:chemistry*; D007259:Infrared Rays; D036103:Nanotechnology; D021241:Spectrometry, Mass, Electrospray Ionization / Q000295:instrumentation / Q000379:methods*; D053719:Tandem Mass Spectrometry
D018834:Chaperonin 60; D001360:Avidin; D000426:Alcohol Dehydrogenase