Surface-Induced Dissociation of Multiply-Protonated Proteins
Citations Over TimeTop 10% of 1995 papers
Abstract
A novel surface design compatible with the open cell geometry allows nonglancing angle collisions of selected ions stored in a Fourier transform mass spectrometer. Dissociation efficiencies of 36%, 22%, and 14% are achieved for gramicidin S, melittin, and carbonic anhydrase (29 kDa), respectively. Ion neutralization by the surface, which is highly competitive for many singly-charged ions, is minimal, and dissociation products of hypervalent neutral species are not detected. Instead, the spectra are similar to those from collisionally activated and infrared multiphoton dissociation; the fragmentation pathways are relatively independent of the method of energy deposition. For carbonic anhydrase, however, the single event excitation inherent to surface-induced dissociation appears to minimize secondary fragmentation, a critical advantage for tandem mass spectrometry of such large ions. Electrically floating the open cell below ground greatly enhances the collection efficiency.
Related Papers
- → Citations Gone #Social: Examining the Effect of Altmetrics on Citations and Readership in Communication Research(2019)27 cited
- → Honoring Native American Code Talkers(2011)5 cited
- → From Attention to Citation, What and How Does Altmetrics Work?(2014)20 cited
- → Literature(1998)1 cited
- Susquehanna Chorale Spring Concert "Roots and Wings"(2017)