Evolution of Structural Biology through the Lens of Mass Spectrometry

Kaur, Upneet; Johnson, Danté T.; Chea, Emily E.; Deredge, Daniel; Espino, Jessica A.; Jones, Lisa M.

doi:10.1021/acs.analchem.8b05014

Cited by 48 publications

(50 citation statements)

References 120 publications

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“…Integration of information from different native and non-native techniques can provide valuable structural insights. 59,60 2.1.2 Collisional activation induces protein unfolding and subunit release. The term 'complex-up' was coined in 2019; 17 however, early examples of subunit release via activation of protein complexes in the gas phase were reported in 1994 by Smith and co-workers.…”

Section: Native Mass Spectrometry Of Protein Complexesmentioning

confidence: 99%

Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry

et al. 2020

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Section: Native Mass Spectrometry Of Protein Complexesmentioning

confidence: 99%

Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry

et al. 2020

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“…Over the last decades bimolecular mass spectrometry (MS), with its ability to analyze low amounts of samples with high speed and sensitivity, has evolved into a central pillar beneficial for integrative structural biology (de Souza and Picotti, 2020;Kaur et al, 2019;Lossl et al, 2016;Robinson, 2019). The structural MS toolbox contains multiple complementary approaches.…”

Section: Introductionmentioning

confidence: 99%

Selective cross-linking of coinciding protein assemblies by in-gel cross-linking mass-spectrometry

Hevler

Lukassen

Cabrera‐Orefice

et al. 2020

Preprint

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Cross-linking mass spectrometry has developed into an important method to study protein structures and interactions. The in-solution cross-linking workflows involve time and sample consuming steps and do not provide sensible solutions for differentiating cross-links obtained from co-occurring protein oligomers, complexes, or conformers. Here we developed a cross-linking workflow combining blue native PAGE with in-gel cross-linking mass spectrometry (IGX-MS). This workflow circumvents steps, such as buffer exchange and cross-linker concentration optimization. Additionally, IGX-MS enables the parallel analysis of co-occurring protein complexes using only small amounts of sample. Another benefit of IGX-MS observed by experiments on GroEL and purified bovine heart mitochondria, is the substantial reduction of artificial over-length cross-links when compared to in-solution cross-linking. We next used IGX-MS to investigate the complement components C5, C6, and their hetero-dimeric C5b6 complex. The obtained cross-links were used to generate a refined structural model of the complement component C6, resembling C6 in its inactivated state. This finding shows that IGX-MS can be used to provide new insights into the initial stages of the terminal complement pathway.

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“…Mass spectrometry (MS)-based proteomics has undergone radical changes since initial studies of proteins by electrospray ionization (ESI) and matrix-assisted laser desorption ionization (MALDI). As new techniques were established, the field of proteomics expanded to analyze protein structure, conformations, and interactions (Kaur et al, 2019). Currently, the field of structural proteomics is experiencing tremendous growth, as newly developed methods, that compliment traditional methods, are continually being assimilated (Table 1).…”

Section: Introductionmentioning

confidence: 99%

The Making of a Footprint in Protein Footprinting: A Review in Honor of Michael L. Gross

McKenzie‐Coe

Shortt

Jones

2020

Mass Spectrometry Reviews

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Within the past decade protein footprinting in conjunction with mass spectrometry has become a powerful and versatile means to unravel the higher order structure of proteins. Footprintingbased approaches has demonstrated the capacity to inform on interaction sites and dynamic regions that participate in conformational changes. These findings when set in a biological perspective inform on protein folding/unfolding, protein-protein interactions, and protein-ligand interactions. In this review, we will look at the contribution of Dr. Michael L. Gross to protein footprinting approaches such as hydrogen deuterium exchange mass spectrometry and hydroxyl radical protein footprinting. This review details the development of novel footprinting methods as well as their applications to study higher order protein structure.

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Evolution of Structural Biology through the Lens of Mass Spectrometry

Cited by 48 publications

References 120 publications

Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry

Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry

Selective cross-linking of coinciding protein assemblies by in-gel cross-linking mass-spectrometry

The Making of a Footprint in Protein Footprinting: A Review in Honor of Michael L. Gross

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