A study of ion-neutral collision cross-section values for low charge states of peptides, proteins, and peptide/protein complexes

Fernandez-Lima, Francisco; Blase, Ryan C.; Russell, David H.

doi:10.1016/j.ijms.2009.10.009

Cited by 40 publications

(46 citation statements)

References 88 publications

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“…With the DMA-MS, we are able to clearly determine protein ion mobilities (in dry air) and masses simultaneously, from which we infer their spherical-equivalent diameters and effective gas-phase densities. We compare our results to those in previous DMA studies as well as to ion diameters inferred from early and recent drift tube IMS-MS measurements in He [4,13,14,38]. Additionally, we demonstrate that the DMA-MS combination can distinguish between protein multimer ions formed nonspecifically during the electrospray process and those formed naturally in solution.…”

Section: Introductionsupporting

confidence: 64%

“…Tables 2 and 3 summarize inferred diameters from mobility measurements for cytochrome C and lysozyme ions, respectively, from this study and prior studies [4,13,14,38,63]. For each measured ion we list the number of protein monomers per ion and the charge state.…”

Section: Protein Diameter and Density Versus Measured Mobilitymentioning

confidence: 99%

“…In all calculations the diameter of the gas molecule is accounted for; it is taken as 0.3 nm for "air" molecules [40] and 0.2 nm for He molecules [64]. Finally, the study to which each data point corresponds [4,13,14,38,63] and the ionization technique used in the study are listed. All other studies used He as a drift gas, and the ionization technique in each study was different (note that we perform ESI under nondenaturing conditions, while strongly denaturing acidic solutions were used in other studies).…”

Section: Protein Diameter and Density Versus Measured Mobilitymentioning

confidence: 99%

“…The IMS-MS combination has recently been used for the identification of aggregates that are undetected by MS alone [2,3], the observation of coulombic stretching of highly charged protein ions [4,5], and to probe gas-phase protein ion structure [6][7][8][9][10][11][12][13][14]. Mobility measurements are particularly interesting in the case of high-mass protein ions generated by electrospray, which are capable of taking on different conformations in the gas phase.…”

Section: Introductionmentioning

confidence: 99%

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Ion Mobility Measurements of Nondenatured 12–150 kDa Proteins and Protein Multimers by Tandem Differential Mobility Analysis–Mass Spectrometry (DMA-MS)

Hogan

Mora

2011

J. Am. Soc. Mass Spectrom.

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The mobilities of electrosprayed proteins and protein multimers with molecular weights ranging from 12.4 kDa (cytochrome C monomers) to 154 kDa (nonspecific concanavalin A hexamers) were measured in dry air by a planar differential mobility analyzer (DMA) coupled to a time-offlight mass spectrometer (TOF-MS). The DMA determines true mobility at atmospheric pressure, without perturbing ion structure from that delivered by the electrospray. A nondenaturing aqueous 20 mM triethylammonium formate buffer yields compact ions with low charge states, moderating polarization effects on ion mobility. Conversion of mobilities into cross-sections involves a reduction factor ξ for the actual mobility relative to that associated with elastic specular collisions with smooth surfaces. ξ is known to be 1.36 in air from Millikan's oil drop experiments. A similar enhancement effect ascribed to atomic-scale surface roughness has been found in numerical simulations. Adopting Millikan's value ξ=1.36 and assuming a spherical geometry yields a gas-phase protein density ρ p =0.949±0.053 g cm −3 for all our protein data. This is substantially higher than the 0.67 g cm −3 found in recent low-resolution DMA measurements of singly charged proteins. DMA-MS can distinguish nonspecific protein aggregates formed during the electrospray process from those formed preferentially in solution.The observed charge versus diameter relation is compatible with a protein charge reduction mechanism based on the evaporation of triethylammonium ions from electrosprayed drops.

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Section: Introductionsupporting

confidence: 64%

Section: Protein Diameter and Density Versus Measured Mobilitymentioning

confidence: 99%

Section: Protein Diameter and Density Versus Measured Mobilitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Ion Mobility Measurements of Nondenatured 12–150 kDa Proteins and Protein Multimers by Tandem Differential Mobility Analysis–Mass Spectrometry (DMA-MS)

Hogan

Mora

2011

J. Am. Soc. Mass Spectrom.

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“…Calibrant ions used were various charge states of insulin (bovine pancreas), ubiquitin (bovine red blood cells), lysozyme, and cytochrome C (horse heart) [35] against the corrected drift times (arrival times) of the corresponding ions measured in TWIM-MS experiments at the same traveling wave velocity, traveling wave height, and ion mobility gas flow settings used for the metallomacrocycles, viz. 350 m/s, 7.5 V, and 22.7 mL/min, respectively.…”

Section: Collision Cross-section Calibrationmentioning

confidence: 99%

Coordination-Driven, Self-Assembly of a Polycyclic, Terpyridine-Based Nanobelt

Xie

Guo

et al. 2016

J Inorg Organomet Polym

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Dendron‐Functionalized Bis(terpyridine)–Iron(II) or –Cadmium(II) Metallomacrocycles: Synthesis, Traveling‐Wave Ion‐Mobility Mass Spectrometry, and Photophysical Properties

Wang

et al. 2011

Chemistry A European J

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The synthesis, purification, structural analysis, and photophysical properties of a series of five-, six-, and seven-sided Fe(II) macrocycles and the corresponding hexameric Cd(II) macrocycle, all prepared by self-assembly of a 120° bis(terpyridine) ligand modified with first- and second-generation 1→3 C-branched dendrons, are reported. All metallomacrocycles were fully characterized by (1)H and (13)C NMR spectroscopy, traveling-wave ion-mobility mass spectrometry (TWIM MS), molecular modeling, UV/Vis absorption spectroscopy, photoluminescence, and cyclic voltammetry. A gradual increase of the collision cross sections of the Fe(II) metallomacrocycles was observed with a successive increase of the number and molecular size of the ligands. The combination of ion-mobility mass spectrometry and NMR techniques unveils structural features that agree well with calculations. Extinction coefficients and emission are significantly modulated by increasing the ring size and changing the metal ion center from Fe(II) to Cd(II) .

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A study of ion-neutral collision cross-section values for low charge states of peptides, proteins, and peptide/protein complexes

Abstract: Here, we report ion-helium collision cross sections (CCS) for a number of peptide, small protein, and peptide/protein ionic complexes.

Cited by 40 publications

References 88 publications

Ion Mobility Measurements of Nondenatured 12–150 kDa Proteins and Protein Multimers by Tandem Differential Mobility Analysis–Mass Spectrometry (DMA-MS)

Ion Mobility Measurements of Nondenatured 12–150 kDa Proteins and Protein Multimers by Tandem Differential Mobility Analysis–Mass Spectrometry (DMA-MS)

Coordination-Driven, Self-Assembly of a Polycyclic, Terpyridine-Based Nanobelt

Dendron‐Functionalized Bis(terpyridine)–Iron(II) or –Cadmium(II) Metallomacrocycles: Synthesis, Traveling‐Wave Ion‐Mobility Mass Spectrometry, and Photophysical Properties

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