GlycoMob: an ion mobility-mass spectrometry collision cross section database for glycomics

2015 ◽  
Vol 33 (3) ◽  
pp. 399-404 ◽  
Author(s):  
Weston B. Struwe ◽  
Kevin Pagel ◽  
Justin L. P. Benesch ◽  
David J. Harvey ◽  
Matthew P. Campbell
Keyword(s):  
Mass Spectrometry ◽  
Cross Section ◽  
Ion Mobility ◽  
Collision Cross Section ◽  
Ion Mobility Mass Spectrometry

scholarly journals Recommendations for Reporting Ion Mobility Mass Spectrometry Measurements

2018 ◽  
Author(s):  
Valerie Gabelica ◽  
Alexandre A. Shvartsburg ◽  
Carlos Afonso ◽  
Perdita E. Barran ◽  
Justin L. P. Benesch ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Cross Section ◽  
Ion Mobility ◽  
Collision Cross Section ◽  
Ion Mobility Mass Spectrometry ◽  
Gas Temperature ◽  
Mobility Data ◽  
Community Effort ◽  
Primary Standards ◽  
Definition Of

Here we present a guide on ion mobility mass spectrometry experiments, which covers both linear and nonlinear methods: what is measured, how the measurements are done, and how to report the results, including the uncertainties on mobility and collision cross section values. The guide aims to clarify some possibly confusing concepts, and the reporting recommendations should help researchers, authors and reviewers to contribute comprehensive reports, so that the ion mobility data can be reused more confidently. Starting from the concept of the definition of the measurand, we emphasize that (i) mobility values (K0) depend intrinsically on ion structure, the nature of the bath gas, temperature, and E/N, (ii) ion mobility does not measure surfaces directly, but collision cross section (CCS) values are derived from mobility values using a physical model, (iii) methods relying on calibration are empirical (and thus may provide method-dependent results) only if the gas nature, temperature or E/N cannot match those of the primary method. Our analysis highlights the urgency of a community effort towards establishing primary standards and reference materials for ion mobility, and provides recommendations to do so. <br><br><br>

Rapid resolution of carbohydrate isomers via multi-site derivatization ion mobility-mass spectrometry

The Analyst ◽  
2018 ◽  
Vol 143 (4) ◽  
pp. 949-955 ◽  
Author(s):  
Li Li ◽  
Kristin R. McKenna ◽  
Zhao Li ◽  
Mahipal Yadav ◽  
Ramanarayanan Krishnamurthy ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Cross Section ◽  
Ion Mobility ◽  
Collision Cross Section ◽  
Ion Mobility Mass Spectrometry ◽  
Rapid Resolution

Identifying small sugar isomers can be challenging by ion mobility-mass spectrometry (IM-MS) alone due to their small collision cross section differences.

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.

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