Electron capture dissociation of polypeptides using a 3 Tesla Fourier transform ion cyclotron resonance mass spectrometer

2002 ◽  
Vol 16 (10) ◽  
pp. 936-943 ◽  
Author(s):  
Nicolas C. Polfer ◽  
Kim F. Haselmann ◽  
Roman A. Zubarev ◽  
Pat R. R. Langridge-Smith



2005 ◽  
Vol 280 (19) ◽  
pp. 19136-19145 ◽  
Author(s):  
Matthew B. Renfrow ◽  
Helen J. Cooper ◽  
Milan Tomana ◽  
Rose Kulhavy ◽  
Yoshiyuki Hiki ◽  
...  








2002 ◽  
Vol 8 (2) ◽  
pp. 177-180 ◽  
Author(s):  
Kathrin Breuker ◽  
HanBin Oh ◽  
Blas A. Cerda ◽  
David M. Horn ◽  
Fred W. McLafferty

In electron-capture dissociation (ECD), a multiply-protonated protein ion, trapped in a Fourier transform-ion cyclotron resonance (FT-ICR) cell, captures a low-energy electron at a protonated site. In a major reaction pathway, the resulting hydrogen atom attacks a backbone carbonyl oxygen to form a hypervalent species that immediately dissociates into a complementary c, z• ion pair. For larger proteins, the reduced odd-electron ion (M + nH)( n −1)+• is a major product, as shown here using isotopically isolated precursors. In addition, a hydrogen atom can be lost without further reaction, yielding the [M + ( n −1)H]( n −1)+ even-electron ions. The large effect of charge state on the yield of these ions suggests that the 9+ to 11+ charge states have novel charge-solvated secondary structures.





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