Coupling Ion Mobility Separations, Collisional Activation Techniques, and Multiple Stages of MS for Analysis of Complex Peptide Mixtures

2002 ◽  
Vol 74 (5) ◽  
pp. 992-1006 ◽  
Author(s):  
Cherokee S. Hoaglund-Hyzer ◽  
Young Jin Lee ◽  
Anne E. Counterman ◽  
David E. Clemmer
Keyword(s):  
Ion Mobility ◽  
Collisional Activation ◽  
Peptide Mixtures ◽  
Multiple Stages

Resolving Isomeric Peptide Mixtures:  A Combined HPLC/Ion Mobility-TOFMS Analysis of a 4000-Component Combinatorial Library

2002 ◽  
Vol 74 (1) ◽  
pp. 26-36 ◽  
Author(s):  
Catherine A. Srebalus Barnes ◽  
Amy E. Hilderbrand ◽  
Stephen J. Valentine ◽  
David E. Clemmer
Keyword(s):  
Ion Mobility ◽  
Combinatorial Library ◽  
Peptide Mixtures

Ion Mobility-Mass Spectrometer Interface for Collisional Activation of Mobility Separated Ions

2009 ◽  
Vol 81 (2) ◽  
pp. 618-624 ◽  
Author(s):  
Francisco A. Fernandez-Lima ◽  
Christopher Becker ◽  
Kent J. Gillig ◽  
William K. Russell ◽  
Shane E. Tichy ◽  
...  
Keyword(s):  
Mass Spectrometer ◽  
Ion Mobility ◽  
Collisional Activation

Development of high-throughput liquid chromatography injected ion mobility quadrupole time-of-flight techniques for analysis of complex peptide mixtures

2002 ◽  
Vol 782 (1-2) ◽  
pp. 343-351 ◽  
Author(s):  
Young Jin Lee ◽  
Cherokee S Hoaglund-Hyzera ◽  
Catherine A Srebalus Barnes ◽  
Amy E Hilderbrand ◽  
Stephen J Valentine ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
High Throughput ◽  
Ion Mobility ◽  
Time Of Flight ◽  
Peptide Mixtures

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 Mass Spectrometric Collisional Activation and Product Ion Mobility of Human Serum Neutral Lipid Extracts

2016 ◽  
Vol 88 (12) ◽  
pp. 6274-6282 ◽  
Author(s):  
Joseph A. Hankin ◽  
Robert M. Barkley ◽  
Karin Zemski-Berry ◽  
Yiming Deng ◽  
Robert C. Murphy
Keyword(s):  
Human Serum ◽  
Neutral Lipid ◽  
Ion Mobility ◽  
Collisional Activation ◽  
Mass Spectrometric
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