Interrogating the Quaternary Structure of Noncanonical Hemoglobin Complexes by Electrospray Mass Spectrometry and Collision-Induced Dissociation

2020 ◽  
Vol 32 (1) ◽  
pp. 270-280
Author(s):  
Alexander I. M. Sever ◽  
Victor Yin ◽  
Lars Konermann
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Mass Spectrometry ◽  
Quaternary Structure ◽  
Collision Induced Dissociation

Collision-Induced Dissociation of Imidazolium-Based Zwitterionic Liquids

2009 ◽  
Vol 15 (4) ◽  
pp. 471-478 ◽  
Author(s):  
Ilva Nakurte ◽  
Peteris Mekss ◽  
Kristaps Klavins ◽  
Andris Zicmanis ◽  
Galina Vavilina ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Mass Spectrometry ◽  
Collision Energy ◽  
Alkyl Chain ◽  
Collision Induced Dissociation ◽  
Cone Voltage ◽  
Fragmentation Pathways ◽  
Fragment Ions ◽  
Molecular Stability ◽  
Imidazolium Ring

Fragmentation pathways of some imidazolium based zwitterionic liquids—3-(3-alkyl-1-imidazolio)-propane sulfonates and 3-(2-methyl-3-alkyl-1-imidazolio)-propane sulfonates—have been studied by tandem electrospray mass spectrometry and collision-induced dissociation. The relative abundances of the lowest energy fragment ions depend on the length of the alkyl chain at the IIN of the imidazolium ring and the cone voltage. The first fragment ions originate from the scission of Cnon aromatic–N bond of compounds investigated, but with increasing collision energy, scission of C–C bonds occurs. Aggregates of the general formula [(M + H) x + (M) y]+ ( x;y = 1–2) formed. Methyl substituted zwitterionic liquids show higher molecular stability than 3-(3-alkyl-1-imidazolio)-propane sulfonates.

Energy-variable collision-induced dissociation study of 1,3,5-trisubstituted 2-pyrazolines by electrospray mass spectrometry

2007 ◽  
Vol 21 (11) ◽  
pp. 1799-1808 ◽  
Author(s):  
Sándor Kéki ◽  
Lajos Nagy ◽  
János Török ◽  
Katalin Tóth ◽  
Albert Lévai ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Mass Spectrometry ◽  
Collision Induced Dissociation ◽  
Energy Variable

Analysis of Trace Level Perchlorate in Drinking Water and Ground Water by Electrospray Mass Spectrometry

1998 ◽  
Author(s):  
Rebecca A. Clewell ◽  
Wayne T. Brashear ◽  
David T. Tsui ◽  
Sanwat Chaudhuri ◽  
Rachel S. Cassady
Keyword(s):  
Mass Spectrometry ◽  
Drinking Water ◽  
Ground Water ◽  
Electrospray Mass Spectrometry ◽  
Trace Level

Current Trends in Biotherapeutic Higher Order Structure Characterization by Irreversible Covalent Footprinting Mass Spectrometry

2019 ◽  
Vol 26 (1) ◽  
pp. 35-43 ◽  
Author(s):  
Natalie K. Garcia ◽  
Galahad Deperalta ◽  
Aaron T. Wecksler
Keyword(s):  
Mass Spectrometry ◽  
Protein Structure ◽  
Protein Interactions ◽  
Quaternary Structure ◽  
Solvent Accessibility ◽  
Higher Order ◽  
Structure Characterization ◽  
Order Structure ◽  
Protein Footprinting ◽  
Wide Range

Background: Biotherapeutics, particularly monoclonal antibodies (mAbs), are a maturing class of drugs capable of treating a wide range of diseases. Therapeutic function and solutionstability are linked to the proper three-dimensional organization of the primary sequence into Higher Order Structure (HOS) as well as the timescales of protein motions (dynamics). Methods that directly monitor protein HOS and dynamics are important for mapping therapeutically relevant protein-protein interactions and assessing properly folded structures. Irreversible covalent protein footprinting Mass Spectrometry (MS) tools, such as site-specific amino acid labeling and hydroxyl radical footprinting are analytical techniques capable of monitoring the side chain solvent accessibility influenced by tertiary and quaternary structure. Here we discuss the methodology, examples of biotherapeutic applications, and the future directions of irreversible covalent protein footprinting MS in biotherapeutic research and development. Conclusion: Bottom-up mass spectrometry using irreversible labeling techniques provide valuable information for characterizing solution-phase protein structure. Examples range from epitope mapping and protein-ligand interactions, to probing challenging structures of membrane proteins. By paring these techniques with hydrogen-deuterium exchange, spectroscopic analysis, or static-phase structural data such as crystallography or electron microscopy, a comprehensive understanding of protein structure can be obtained.

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