Rapid 3-dimensional shape determination of globular proteins by mobility capillary electrophoresis and native mass spectrometry

Wu, Haimei; Zhang, Rongkai; Zhang, Wenjing; Hong, Jie; Xiang, Ye; Xu, Wei

doi:10.1039/d0sc01965h

Cited by 23 publications

(27 citation statements)

References 85 publications

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“…However, significant deviations between theoretical and experimental CCS have been observed in some proteins, and are commonly caused by the collapse of unsupported or disordered structures. ,− Interestingly, a recent report outlined how a combination of capillary electrophoresis and native MS can provide comparable insights into protein shapes. The approach is likely similarly sensitive to desolvation-related structural changes . We, therefore, considered how gas-phase changes in protein structures affect the ability to predict the shape of a protein complex.…”

Section: Resultsmentioning

confidence: 99%

“…The approach is likely similarly sensitive to desolvation-related structural changes. 34 We, therefore, considered how gas-phase changes in protein structures affect the ability to predict the shape of a protein complex. As a test case, we selected the ferritin from Archaeoglobus f ulgidus, a homo-24-mer that forms a hollow sphere with four large pores and which partially collapses in the gas phase.…”

Section: Analytical Chemistrymentioning

confidence: 99%

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Predicting the Shapes of Protein Complexes through Collision Cross Section Measurements and Database Searches

et al. 2020

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In structural biology, collision cross sections (CCS) from ion mobility mass spectrometry (IM-MS) measurements are routinely compared to computationally or experimentally derived protein structures. Here, we investigate whether CCS data can inform about the shape of a protein in the absence of specific reference structures. Analysis of the proteins in the CCS database shows that protein complexes with low apparent densities are structurally more diverse than those with a high apparent density. Using the CCS, molecular weight, and oligomeric states to mine the Protein Data Bank (PDB) for potentially similar protein structures, we find that we can distinguish oblate-and prolate-shaped protein complexes. We then apply the strategy to an integral membrane protein by comparing the shapes of a prokaryotic and an eukaryotic sodium/proton antiporter homologue. We conclude that mining the PDB with IM-MS data is a time-effective way to derive low-resolution structural models. File list (2) download file view on ChemRxiv main_chemrxiv.docx (2.05 MiB) download file view on ChemRxiv Supplementary Tables 1-4.pdf (50.74 KiB)

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Section: Resultsmentioning

confidence: 99%

Section: Analytical Chemistrymentioning

confidence: 99%

Predicting the Shapes of Protein Complexes through Collision Cross Section Measurements and Database Searches

et al. 2020

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“…Under optimized conditions, this design enhanced the ion signal intensity by~10 times, compared to a commercial nanoESI source, with the LODs for peptides reaching 1 mg/mL to~20 μg/mL. Similarly, a new medium throughput method was developed to couple MCE with native MS for protein analysis [68]. In this design, Tayler dispersion analysis (TDA) that provides the determination of the diffusion coefficient of analytes was integrated into MCE, allowing the measurement of ion separation, hydrodynamic radius, and effective charge in a single experiment (Fig.…”

Section: Mass Spectrometry (Ms)mentioning

confidence: 99%

Recent (2018–2020) development in capillary electrophoresis

Gao

Zhong

2021

Anal Bioanal Chem

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Development of new capillary electrophoresis (CE) methodology and instrumentation, as well as application of CE to solve new problems, remains an active research area because of the attractive features of CE compared to other separation techniques. In this review, we focus on the representative works about sample preconcentration, separation media or capillary coating development, detector construction, and multidimensional separation in CE, which are judiciously selected from the papers published in 2018-2020.

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“…reviewed advances in CE‐MS for proteomics analysis [70]. The bimolecular 3D structure was analyzed with mobility CE using MS detection [71, 72]. The mobility CE coupled with MS has also been used for the determination of the charge state of proteins [73].…”

Section: Detectionmentioning

confidence: 99%

Recent advances in the analysis of plant alkaloids by capillary electrophoresis and micellar electrokinetic chromatography

Kumar

Malik

Singh

2021

Separation Science Plus

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Plants produce secondary metabolites as a result of a defense mechanism of plants against biotic and abiotic stresses. Alkaloids represent a diverse group of secondary metabolites that contain a basic nitrogen atom. Capillary electrophoresis has many advantages such as short analysis time, little sample consumption, high separation efficiency, and high sensitivity over conventional separation methods. Therefore, capillary electrophoresis has been extensively used for the analysis of alkaloids in plant extracts. In this review, we discuss advances in analytical capillary electrophoresis used for their identification and quantification in plants.

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Rapid 3-dimensional shape determination of globular proteins by mobility capillary electrophoresis and native mass spectrometry

Abstract: Using native mass spectrometry and mobility capillary electrophoresis, the ellipsoid dimensions of globular proteins or protein complexes could be measured efficiently.

Cited by 23 publications

References 85 publications

Predicting the Shapes of Protein Complexes through Collision Cross Section Measurements and Database Searches

Predicting the Shapes of Protein Complexes through Collision Cross Section Measurements and Database Searches

Recent (2018–2020) development in capillary electrophoresis

Recent advances in the analysis of plant alkaloids by capillary electrophoresis and micellar electrokinetic chromatography

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