Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool

Native mass spectrometry (nMS) is evolving into a workhorse for structural biology. The plethora of online and offline preparation, separation, and purification methods as well as numerous ionization techniques combined with powerful new hybrid ion mobility and mass spectrometry systems has illustra...

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Bibliographic Details
Published in:Chemical reviews 2022-04, Vol.122 (8), p.7442-7487
Main Authors: Snyder, Dalton T, Harvey, Sophie R, Wysocki, Vicki H
Format: Article
Language:English
Subjects:
Biology
Cryoelectron Microscopy
Crystal structure
Humans
Ionic mobility
Ionization
Ions
Mass spectrometry
Proteins
Proteins - chemistry
Scientific imaging
Spectroscopy
Tandem Mass Spectrometry - methods
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Summary:Native mass spectrometry (nMS) is evolving into a workhorse for structural biology. The plethora of online and offline preparation, separation, and purification methods as well as numerous ionization techniques combined with powerful new hybrid ion mobility and mass spectrometry systems has illustrated the great potential of nMS for structural biology. Fundamental to the progression of nMS has been the development of novel activation methods for dissociating proteins and protein complexes to deduce primary, secondary, tertiary, and quaternary structure through the combined use of multiple MS/MS technologies. This review highlights the key features and advantages of surface collisions (surface-induced dissociation, SID) for probing the connectivity of subunits within protein and nucleoprotein complexes and, in particular, for solving protein structure in conjunction with complementary techniques such as cryo-EM and computational modeling. Several case studies highlight the significant role SID, and more generally nMS, will play in structural elucidation of biological assemblies in the future as the technology becomes more widely adopted. Cases are presented where SID agrees with solved crystal or cryoEM structures or provides connectivity maps that are otherwise inaccessible by “gold standard” structural biology techniques.
ISSN:0009-2665
1520-6890
1520-6890
DOI:10.1021/acs.chemrev.1c00309