Electron transfer with no dissociation ion mobility–mass spectrometry (ETnoD IM-MS). The effect of charge reduction on protein conformation

Jhingree, Jacquelyn; Beveridge, Rebecca; Dickinson, Eleanor R.; Williams, Jonathan P.; Brown, Jeffery M.; Bellina, Bruno; Barran, Perdita E.

doi:10.1016/j.ijms.2016.08.006

Cited by 28 publications

(54 citation statements)

References 51 publications

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“… 312 − 314 Jhingree et al performed similar experiments but used ETnoD products instead of PTR products to study the effects of charge reduction on protein structure. 315 Moreover, the Sobott group investigated how ETD and PTR can be balanced to generate sequencing ions and spectral decongestion. 316 …”

Section: Other Uses Of Etd and Related Ion–ion Reactionsmentioning

confidence: 99%

The Role of Electron Transfer Dissociation in Modern Proteomics

2017

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Section: Other Uses Of Etd and Related Ion–ion Reactionsmentioning

confidence: 99%

The Role of Electron Transfer Dissociation in Modern Proteomics

2017

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“…5,18,19 In contrast, stronger relationships between Ω and z have been reported for native-like ions of smaller proteins, 20,21 prion and intrinsically disordered proteins, 22,23 and proteins generated from solutions with “supercharging” reagents, 24 as well as protein ions from denaturing solutions. 25–27 Thus, it is unclear from IM-MS measurements alone the extent to which the z of a native-like ion affects its structure, and whether low- z ions have “more native” structures. As a result, several approaches to report Ω with respect to z have been implemented that each implicitly assume different relationships between z and the structure of a native-like ion, including reporting a Ω for each z measured, 5,18 reporting an average Ω, 28 and extrapolating to the Ω of a “zero-charge” protein.…”

Section: Introductionmentioning

confidence: 99%

Interpreting the Collision Cross Sections of Native-like Protein Ions: Insights from Cation-to-Anion Proton-Transfer Reactions

Laszlo

Bush

2017

Anal. Chem.

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The effects of charge state on structures of native-like cations of serum albumin, streptavidin, avidin, and alcohol dehydrogenase were probed using cation-to-anion proton-transfer reactions (CAPTR), ion mobility, mass spectrometry, and complementary energy-dependent experiments. The CAPTR products all have collision cross section (Ω) values that are within 5.5% of the original precursor cations. The first CAPTR event for each precursor yields products that have smaller Ω values and frequently exhibit the greatest magnitude of change in Ω resulting from a single CAPTR event. To investigate how the structures of the precursors affect the structures of the products, ions were activated as a function of energy prior to CAPTR. In each case, the Ω of the activated precursors increase with increasing energy, but the Ω of the CAPTR products are smaller than the activated precursors. To investigate the stabilities of the CAPTR products, the products were activated immediately prior to ion mobility. These results show that additional structures with smaller or larger Ω can be populated and that the structures and stabilities of these ions depend most strongly on the identity of the protein and the charge state of the product, rather than the charge state of the precursor or the number of CAPTR events. Together, these results indicate that the excess charges initially present on native-like ions have a modest, but sometimes statistically significant, effect on their Ω values. Therefore, potential contributions from charge state should be considered when using experimental Ω values to elucidate structures in solution.

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“…IM-MS has been utilised to study the conformational landscapes of mono-and homo-oligomeric proteins, 6 protein-protein 7 and protein-ligand complexes. 4, [8][9][10] In addition to gas phase separation, MS and IM-MS has been used to study biophysical phenomena such as gas phase protein rearrangement, 8 stabilisation and rearrangement of protein ensembles upon ligand binding, 8,11 proton-and electron 3 | P a g e transfer mechanisms 12,13 and protein unfolding 4, 14,15 , with the latter becoming increasingly more popular.…”

Section: Introductionmentioning

confidence: 99%

ORIGAMI: A Software Suite for Activated Ion Mobility Mass Spectrometry (aIM-MS) Applied To Multimeric Protein Assemblies

Migas

Bellina

Barran

2017

Preprint

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We present here a software suite (ORIGAMI) that facilitates the rapid acquisition and analysis of ion mobility data following collisional activation. ORIGAMI was developed for use on Waters Synapt instruments where data acquisition is achieved by interfacing WREnS (Waters Research Enabled Software) and MassLynx. Two components are presented, the first is ORIGAMI MS 20, 2017; 2 | P a g e statistical analysis and figure creation capabilities. We demonstrate the use of ORIGAMI on concanavalin A and alcohol dehydrogenase acquired using the traditional protocols and thenot peer-reviewed) is the author/funder. It is made available under a The copyright holder for this preprint (which was . http://dx.doi.org/10.1101/152686 doi: bioRxiv preprint first posted online Jun. ORIGAMIMS method. Highlights-New methodology for faster acquisition and data analysis following activation of ions separated by ion mobility mass spectrometry -Software package capable of simultaneous analysis of multiple MassLynx .raw files -Visualization of the change in mobility of parent and fragment ions following activation -Easy extraction, data processing and extensive plotting tools

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Electron transfer with no dissociation ion mobility–mass spectrometry (ETnoD IM-MS). The effect of charge reduction on protein conformation

Cited by 28 publications

References 51 publications

The Role of Electron Transfer Dissociation in Modern Proteomics

The Role of Electron Transfer Dissociation in Modern Proteomics

Interpreting the Collision Cross Sections of Native-like Protein Ions: Insights from Cation-to-Anion Proton-Transfer Reactions

ORIGAMI: A Software Suite for Activated Ion Mobility Mass Spectrometry (aIM-MS) Applied To Multimeric Protein Assemblies

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