scholarly journals Editorial: Focus on Protein Footprinting, Honoring Michael Gross, Recipient of the 2020 John B. Fenn Award for a Distinguished Contribution in Mass Spectrometry

2021 ◽  
Vol 32 (7) ◽  
pp. 1565-1566
Author(s):  
Joseph A. Loo ◽  
David H. Russell ◽  
Yinsheng Wang
Keyword(s):  
Mass Spectrometry ◽  
Protein Footprinting ◽  
Distinguished Contribution

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.

scholarly journals Protein Footprinting Comes of Age: Mass Spectrometry for Biophysical Structure Assessment

2017 ◽  
Vol 16 (5) ◽  
pp. 706-716 ◽  
Author(s):  
Liwen Wang ◽  
Mark R. Chance
Keyword(s):  
Mass Spectrometry ◽  
Protein Footprinting ◽  
Structure Assessment

scholarly journals Probing Conformational Changes of Human DNA Polymerase λ using Mass Spectrometry-Based Protein Footprinting

2009 ◽  
Vol 390 (3) ◽  
pp. 368-379 ◽  
Author(s):  
Jason D. Fowler ◽  
Jessica A. Brown ◽  
Mamuka Kvaratskhelia ◽  
Zucai Suo
Keyword(s):  
Mass Spectrometry ◽  
Dna Polymerase ◽  
Conformational Changes ◽  
Protein Footprinting ◽  
Human Dna ◽  
Dna Polymerase Λ

scholarly journals Mass Spectrometry-Based Protein Footprinting Characterizes the Structures of Oligomeric Apolipoprotein E2, E3, and E4

Biochemistry ◽  
2011 ◽  
Vol 50 (38) ◽  
pp. 8117-8126 ◽  
Author(s):  
Brian Gau ◽  
Kanchan Garai ◽  
Carl Frieden ◽  
Michael L. Gross
Keyword(s):  
Mass Spectrometry ◽  
Protein Footprinting

ChemInform Abstract: Advances in Radical Probe Mass Spectrometry for Protein Footprinting in Chemical Biology Applications

ChemInform ◽  
2014 ◽  
Vol 45 (26) ◽  
pp. no-no
Author(s):  
Simin D. Maleknia ◽  
Kevin M. Downard
Keyword(s):  
Mass Spectrometry ◽  
Chemical Biology ◽  
Protein Footprinting
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