Positive and negative electrospray ionisation travelling wave ion mobility mass spectrometry and low-energy collision-induced dissociation of sialic acid derivatives

2011 ◽  
Vol 25 (21) ◽  
pp. 3235-3244 ◽  
Author(s):  
Wolfgang Winkler ◽  
Wolfgang Huber ◽  
Reinhard Vlasak ◽  
Günter Allmaier
Keyword(s):  
Mass Spectrometry ◽  
Sialic Acid ◽  
Ion Mobility ◽  
Travelling Wave ◽  
Low Energy ◽  
Collision Induced Dissociation ◽  
Ion Mobility Mass Spectrometry ◽  
Energy Collision ◽  
Electrospray Ionisation

scholarly journals Amphitrite: A program for processing travelling wave ion mobility mass spectrometry data

2013 ◽  
Vol 345-347 ◽  
pp. 54-62 ◽  
Author(s):  
Ganesh N. Sivalingam ◽  
Jun Yan ◽  
Harpal Sahota ◽  
Konstantinos Thalassinos
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Travelling Wave ◽  
Mass Spectrometry Data ◽  
Ion Mobility Mass Spectrometry

Characterisation of Calmodulin Structural Transitions by Ion Mobility Mass Spectrometry

2012 ◽  
Vol 65 (5) ◽  
pp. 504 ◽  
Author(s):  
Antonio N. Calabrese ◽  
Lauren A. Speechley ◽  
Tara L. Pukala
Keyword(s):  
Mass Spectrometry ◽  
Cross Section ◽  
Cross Sections ◽  
Ion Mobility ◽  
Collision Cross Section ◽  
Travelling Wave ◽  
Ion Mobility Mass Spectrometry ◽  
Structural Transitions ◽  
Calmodulin Binding ◽  
Negative Mode

This study demonstrates the ability of travelling wave ion mobility-mass spectrometry to measure collision cross-sections of ions in the negative mode, using a calibration based approach. Here, negative mode ion mobility-mass spectrometry was utilised to understand structural transitions of calmodulin upon Ca2+ binding and complexation with model peptides melittin and the plasma membrane Ca2+ pump C20W peptide. Coexisting calmodulin conformers were distinguished on the basis of their mass and cross-section, and identified as relatively folded and unfolded populations, with good agreement in collision cross-section to known calmodulin geometries. Titration of calcium tartrate to physiologically relevant Ca2+ levels provided evidence for intermediately metalated species during the transition from apo- to holo-calmodulin, with collision cross-section measurements indicating that higher Ca2+ occupancy is correlated with more compact structures. The binding of two representative peptides which exemplify canonical compact (melittin) and extended (C20W) peptide-calmodulin binding models has also been interrogated by ion mobility mass spectrometry. Peptide binding to calmodulin involves intermediates with metalation states from 1–4 Ca2+, which demonstrate relatively collapsed structures, suggesting neither the existence of holo-calmodulin or a pre-folded calmodulin conformation is a prerequisite for binding target peptides or proteins. The biological importance of the different metal unsaturated calmodulin complexes, if any, is yet to be understood.

Detection of a Protein Conformational Equilibrium by Electrospray Ionisation-Ion Mobility-Mass Spectrometry

2011 ◽  
Vol 123 (36) ◽  
pp. 8441-8444 ◽  
Author(s):  
Matthew Jenner ◽  
Jacqueline Ellis ◽  
Wei-Cheng Huang ◽  
Emma Lloyd Raven ◽  
Gordon C. K. Roberts ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Conformational Equilibrium ◽  
Ion Mobility Mass Spectrometry ◽  
Electrospray Ionisation

Detection of a Protein Conformational Equilibrium by Electrospray Ionisation-Ion Mobility-Mass Spectrometry

2011 ◽  
Vol 50 (36) ◽  
pp. 8291-8294 ◽  
Author(s):  
Matthew Jenner ◽  
Jacqueline Ellis ◽  
Wei-Cheng Huang ◽  
Emma Lloyd Raven ◽  
Gordon C. K. Roberts ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Conformational Equilibrium ◽  
Ion Mobility Mass Spectrometry ◽  
Electrospray Ionisation
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