Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/115907
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Type: Journal article
Title: Conditions for analysis of native protein structures using uniform field drift tube ion mobility mass spectrometry and characterization of stable calibrants for TWIM-MS
Author: Harrison, J.A.
Kelso, C.
Pukala, T.L.
Beck, J.L.
Citation: Journal of The American Society for Mass Spectrometry, 2019; 30(2):256-267
Publisher: Springer US
Issue Date: 2019
ISSN: 1044-0305
1879-1123
Statement of
Responsibility: 
Julian A. Harrison, Celine Kelso, Tara L. Pukala, Jennifer L. Beck
Abstract: Determination of collisional cross sections (CCS) by travelling wave ion mobility mass spectrometry (TWIM-MS) requires calibration against standards for which the CCS has been measured previously by drift tube ion mobility mass spectrometry (DTIM-MS). The different extents of collisional activation in TWIM-MS and DTIM-MS can give rise to discrepancies in the CCS of calibrants across the two platforms. Furthermore, the conditions required to ionize and transmit large, folded proteins and assemblies may variably affect the structure of the calibrants and analytes. Stable hetero-oligomeric phospholipase A2 (PDx) and its subunits were characterized as calibrants for TWIM-MS. Conditions for acquisition of native-like TWIM (Synapt G1 HDMS) and DTIM (Agilent 6560 IM-Q-TOF) mass spectra were optimized to ensure the spectra exhibited similar charge state distributions. CCS measurements (DTIM-MS) for ubiquitin, cytochrome c, holo-myoglobin, serum albumin and glutamate dehydrogenase were in good agreement with other recent results determined using this and other DTIM-MS instruments. PDx and its β and γ subunits were stable across a wide range of cone and trap voltages in TWIM-MS and were stable in the presence of organic solvents. The CCS of PDx and its subunits were determined by DTIM-MS and were used as calibrants in determination of CCS of native-like cytochrome c, holo-myoglobin, carbonic anhydrase, serum albumin and haemoglobin in TWIM-MS. The CCS values were in good agreement with those measured by DTIM-MS where available. These experiments demonstrate conditions for analysis of native-like proteins using a commercially available DTIM-MS instrument, characterize robust calibrants for TWIM-MS, and present CCS values determined by DTIM-MS and TWIM-MS for native proteins to add to the current literature database. Graphical Abstract ᅟ.
Keywords: Native mass spectrometry; Drift tube ion mobility mass spectrometry; Travelling wave ion mobility mass spectrometry
Description: Published online: 15 October 2018
Rights: © American Society for Mass Spectrometry, 2018
RMID: 0030100581
DOI: 10.1007/s13361-018-2074-z
Grant ID: http://purl.org/au-research/grants/arc/LE0882289
Appears in Collections:Chemistry publications

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