Electron capture and transfer dissociation: Peptide structure analysis at different ion internal energy levels |
| |
Authors: | Hisham Ben Hamidane Diego Chiappe Ralf Hartmer Aleksey Vorobyev Marc Moniatte Yury O Tsybin |
| |
Institution: | 1. Ecole Polytechnique Fédérale de Lausanne, Biomolecular Mass Spectrometry Laboratory, BCH 4307, 1015, Lausanne, Switzerland 2. Proteomics Core Facility, Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland 3. Bruker Daltonics GmbH, Bremen, Germany
|
| |
Abstract: | We decoupled electron-transfer dissociation (ETD) and collision-induced dissociation of charge-reduced species (CRCID) events
to probe the lifetimes of intermediate radical species in ETD-based ion trap tandem mass spectrometry of peptides. Short-lived
intermediates formed upon electron transfer require less energy for product ion formation and appear in regular ETD mass spectra,
whereas long-lived intermediates require additional vibrational energy and yield product ions as a function of CRCID amplitude.
The observed dependencies complement the results obtained by double-resonance electron-capture dissociation (ECD) Fourier
transform ion cyclotron resonance mass spectrometry (FT-ICR MS) and ECD in a cryogenic ICR trap. Compared with ECD FT-ICR
MS, ion trap MS offers lower precursor ion internal energy conditions, leading to more abundant charge-reduced radical intermediates
and larger variation of product ion abundance as a function of vibrational post-activation amplitude. In many cases decoupled
CRCID after ETD exhibits abundant radical c-type and even-electron z-type ions, in striking contrast to predominantly even-electron c-type and radical z-type ions in ECD FT-ICR MS and especially activated ion-ECD, thus providing a new insight into the fundamentals of ECD/ETD. |
| |
Keywords: | |
本文献已被 ScienceDirect SpringerLink 等数据库收录! |
|