scholarly journals Characterization of Protein Structure with Ion Mobility Mass Spectrometry, Multiplexed Fragmentation Strategies and Data Directed Analysis

2020 ◽  
Author(s):  
Rachelle Black ◽  
Alexey Barkhanskiy ◽  
Lennart Ramakers ◽  
Alina Theisen ◽  
Jeffery Brown ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Collisional Activation ◽  
A Priori ◽  
Data Driven ◽  
Ion Mobility Mass Spectrometry ◽  
Backbone Cleavage ◽  
Fragmentation Pattern ◽  
Mobility Separation ◽  
Folded Structure

<p>Activated ion mobility measurements provide Insights to the stability of tertiary and quaternary structures of proteins and pairing such approaches with fragmentation can delineate which part(s) of the primary sequence are disrupted from a folded structure. In this work we use 213 nm photodissociation coupled with ion mobility mass spectrometry and collisional activation to determine the conformational landscape of model proteins. UVPD experiments are performed on proteins following in source activation as well as on collisionally activated photoproducts post ion mobility separation. For cytochrome c, there is a significant increase in the fragmentation yield with collisional activation post mobility, for all conformational states. Similar strategies are deployed with the model multimeric proteins, concanavalin a, and haemoglobin. For these complexes’ CID leads to classic asymmetric charge distribution in subunit products, which when preceded by UV irradiation yields fragments from within the sub-unit that can be mapped to the quaternary fold. Data driven, multivariate analysis (MVA) was used to determine the significant differences in UVPD and CID fragmentation pattern following in source activation. This data driven approach reveals diagnostic fragments without <i>a priori</i> assignments limited to predicated backbone cleavage and provides a new approach to map conformation landscapes that may have wider utility.</p>

scholarly journals Characterization of Protein Structure with Ion Mobility Mass Spectrometry, Multiplexed Fragmentation Strategies and Data Directed Analysis

2020 ◽  
Author(s):  
Rachelle Black ◽  
Alexey Barkhanskiy ◽  
Lennart Ramakers ◽  
Alina Theisen ◽  
Jeffery Brown ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Collisional Activation ◽  
A Priori ◽  
Data Driven ◽  
Ion Mobility Mass Spectrometry ◽  
Backbone Cleavage ◽  
Fragmentation Pattern ◽  
Mobility Separation ◽  
Folded Structure

<p>Activated ion mobility measurements provide Insights to the stability of tertiary and quaternary structures of proteins and pairing such approaches with fragmentation can delineate which part(s) of the primary sequence are disrupted from a folded structure. In this work we use 213 nm photodissociation coupled with ion mobility mass spectrometry and collisional activation to determine the conformational landscape of model proteins. UVPD experiments are performed on proteins following in source activation as well as on collisionally activated photoproducts post ion mobility separation. For cytochrome c, there is a significant increase in the fragmentation yield with collisional activation post mobility, for all conformational states. Similar strategies are deployed with the model multimeric proteins, concanavalin a, and haemoglobin. For these complexes’ CID leads to classic asymmetric charge distribution in subunit products, which when preceded by UV irradiation yields fragments from within the sub-unit that can be mapped to the quaternary fold. Data driven, multivariate analysis (MVA) was used to determine the significant differences in UVPD and CID fragmentation pattern following in source activation. This data driven approach reveals diagnostic fragments without <i>a priori</i> assignments limited to predicated backbone cleavage and provides a new approach to map conformation landscapes that may have wider utility.</p>

scholarly journals MALDI-ion mobility mass spectrometry of lipids in negative ion mode

2014 ◽  
Vol 6 (14) ◽  
pp. 5001-5007 ◽  
Author(s):  
Shelley N. Jackson ◽  
Damon Barbacci ◽  
Thomas Egan ◽  
Ernest K. Lewis ◽  
J. Albert Schultz ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Negative Ion ◽  
Ion Mobility Mass Spectrometry ◽  
Maldi Imaging ◽  
Mobility Separation ◽  
Ion Mobility Separation ◽  
Negative Ion Mode

Ion mobility separation of two lipids prior to MALDI imaging.

scholarly journals Ion mobility separation of deprotonated oligosaccharide isomers – evidence for gas-phase charge migration

2016 ◽  
Vol 52 (83) ◽  
pp. 12353-12356 ◽  
Author(s):  
W. B. Struwe ◽  
C. Baldauf ◽  
J. Hofmann ◽  
P. M. Rudd ◽  
K. Pagel
Keyword(s):  
Mass Spectrometry ◽  
Gas Phase ◽  
Quantum Chemical Calculations ◽  
Ion Mobility ◽  
Quantum Chemical ◽  
Ion Mobility Mass Spectrometry ◽  
Charge Migration ◽  
Mobility Separation ◽  
Ion Mobility Separation

Ion mobility-mass spectrometry in combination with quantum chemical calculations provides evidence that the charge in deprotonated glycan ions is mobile.

Rapid Diagnosis of Parkinson’s Disease from Sebum using Paper Spray Ionisation Ion Mobility Mass Spectrometry

2020 ◽  
Author(s):  
Depanjan Sarkar ◽  
Drupad Trivedi ◽  
Eleanor Sinclair ◽  
Sze Hway Lim ◽  
Caitlin Walton-Doyle ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Ion Mobility ◽  
Neurodegenerative Disorder ◽  
Treatment Options ◽  
Ion Mobility Mass Spectrometry ◽  
Paper Spray ◽  
Molecular Features ◽  
Validation Set

Parkinson’s disease (PD) is the second most common neurodegenerative disorder for which identification of robust biomarkers to complement clinical PD diagnosis would accelerate treatment options and help to stratify disease progression. Here we demonstrate the use of paper spray ionisation coupled with ion mobility mass spectrometry (PSI IM-MS) to determine diagnostic molecular features of PD in sebum. PSI IM-MS was performed directly from skin swabs, collected from 34 people with PD and 30 matched control subjects as a training set and a further 91 samples from 5 different collection sites as a validation set. PSI IM-MS elucidates ~ 4200 features from each individual and we report two classes of lipids (namely phosphatidylcholine and cardiolipin) that differ significantly in the sebum of people with PD. Putative metabolite annotations are obtained using tandem mass spectrometry experiments combined with accurate mass measurements. Sample preparation and PSI IM-MS analysis and diagnosis can be performed ~5 minutes per sample offering a new route to for rapid and inexpensive confirmatory diagnosis of this disease.

Spatial Metabolomics of the Human Kidney Using MALDI Trapped Ion Mobility Imaging Mass Spectrometry

2020 ◽  
Author(s):  
Elizabeth Neumann ◽  
Lukasz Migas ◽  
Jamie L. Allen ◽  
Richard Caprioli ◽  
Raf Van de Plas ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Imaging Mass Spectrometry ◽  
Structural Complexity ◽  
Human Kidney ◽  
Resolving Power ◽  
Mobility Separation ◽  
Trapped Ion ◽  
Mobility Data ◽  
Ion Mobility Separation

<div> <div> <p>Small metabolites are essential for normal and diseased biological function but are difficult to study because of their inherent structural complexity. MALDI imaging mass spectrometry (IMS) of small metabolites is particularly challenging as MALDI matrix clusters are often isobaric with metabolite ions, requiring high resolving power instrumentation or derivatization to circumvent this issue. An alternative to this is to perform ion mobility separation before ion detection, enabling the visualization of metabolites without the interference of matrix ions. Here, we use MALDI timsTOF IMS to image small metabolites at high spatial resolution within the human kidney. Through this, we have found metabolites, such as arginic acid, acetylcarnitine, and choline that localize to the cortex, medulla, and renal pelvis, respectively. We have also demonstrated that trapped ion mobility spectrometry (TIMS) can resolve matrix peaks from metabolite signal and separate both isobaric and isomeric metabolites with different localizations within the kidney. The added ion mobility data dimension dramatically increased the peak capacity for molecular imaging experiments. Future work will involve further exploring the small metabolite profiles of human kidneys as a function of age, gender, and ethnicity.</p></div></div>

P‐97: Separation of Isomeric OLED Materials Using Ion Mobility‐Mass Spectrometry (IM‐MS)

2021 ◽  
Vol 52 (1) ◽  
pp. 1444-1447
Author(s):  
Hirotaka Shioji ◽  
Azusa Uematsu ◽  
Motoshi Onoda ◽  
Keiko Matsuda ◽  
Keisuke Sawada ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Ion Mobility Mass Spectrometry
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