Letter: Evaluation and comparison of collision-induced dissociation and electron-capture dissociation for top-down analysis of intact ribonuclease B

2015 ◽  
Vol 21 (4) ◽  
pp. 707 ◽  
Author(s):  
Ze Wang ◽  
Xiangfeng Chen ◽  
Liulin Deng ◽  
Wan Li ◽  
Y.-L. Elaine Wong ◽  
...  
Keyword(s):  
Electron Capture ◽  
Electron Capture Dissociation ◽  
Collision Induced Dissociation ◽  
Top Down ◽  
Ribonuclease B

scholarly journals Electron capture dissociation and drift tube ion mobility-mass spectrometry coupled with site directed mutations provide insights into the conformational diversity of a metamorphic protein

2015 ◽  
Vol 17 (16) ◽  
pp. 10538-10550 ◽  
Author(s):  
Sophie R. Harvey ◽  
Massimiliano Porrini ◽  
Robert C. Tyler ◽  
Cait E. MacPhee ◽  
Brian F. Volkman ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Electron Capture ◽  
Electron Capture Dissociation ◽  
Ion Mobility ◽  
Drift Tube ◽  
Ion Mobility Mass Spectrometry ◽  
Top Down ◽  
Conformational Diversity ◽  
Metamorphic Protein

Ion mobility mass spectrometry can be combined with data from top-down sequencing to discern adopted conformations of proteins in the absence of solvent.

scholarly journals Electron capture dissociation mass spectrometric analysis of lysine-phosphorylated peptides

2010 ◽  
Vol 30 (6) ◽  
pp. 433-443 ◽  
Author(s):  
Karolina Kowalewska ◽  
Piotr Stefanowicz ◽  
Tomasz Ruman ◽  
Tomasz Frączyk ◽  
Wojciech Rode ◽  
...  
Keyword(s):  
Electron Capture ◽  
Electron Capture Dissociation ◽  
31P Nmr ◽  
Basic Amino Acid ◽  
Collision Induced Dissociation ◽  
Spectrometric Analysis ◽  
Phosphorylation Sites ◽  
Nmr Studies ◽  
Phosphorylated Peptides ◽  
Phosphorylation Reaction

Phosphorylation of proteins is an essential signalling mechanism in eukaryotic and prokaryotic cells. Although N-phosphorylation of basic amino acid is known for its importance in biological systems, it is still poorly explored in terms of products and mechanisms. In the present study, two MS fragmentation methods, ECD (electron-capture dissociation) and CID (collision-induced dissociation), were tested as tools for analysis of N-phosphorylation of three model peptides, RKRSRAE, RKRARKE and PLSRTLSVAAKK. The peptides were phosphorylated by reaction with monopotassium phosphoramidate. The results were confirmed by 1H NMR and 31P NMR studies. The ECD method was found useful for the localization of phosphorylation sites in unstable lysine-phosphorylated peptides. Its main advantage is a significant reduction of the neutral losses related to the phosphoramidate moiety. Moreover, the results indicate that the ECD–MS may be useful for analysis of regioselectivity of the N-phosphorylation reaction. Stabilities of the obtained lysine-phosphorylated peptides under various conditions were also tested.

scholarly journals Mapping a Noncovalent Protein–Peptide Interface by Top-Down FTICR Mass Spectrometry Using Electron Capture Dissociation

2011 ◽  
Vol 22 (8) ◽  
pp. 1432-1440 ◽  
Author(s):  
David J. Clarke ◽  
Euan Murray ◽  
Ted Hupp ◽  
C. Logan Mackay ◽  
Pat R. R. Langridge-Smith
Keyword(s):  
Mass Spectrometry ◽  
Electron Capture ◽  
Electron Capture Dissociation ◽  
Top Down ◽  
Fticr Mass Spectrometry ◽  
Noncovalent Protein
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