Ion Mobility-Mass Spectrometry: Time-Dispersive Instrumentation

May, Jody C.; McLean, John A.

doi:10.1021/ac504720m

Cited by 364 publications

(367 citation statements)

References 212 publications

(336 reference statements)

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“…These include spectroscopic tools [12][13][14], dissociation experiments [5,6,8], gas phase H/D exchange [15,16], soft landing/EM [4,17], and computer simulations [10,[18][19][20]. The technique that is currently most widely used for characterizing biomolecular conformations in the gas phase is ion mobility spectrometry (IMS) [21][22][23][24][25][26][27].…”

Section: Introductionmentioning

confidence: 99%

Protein Structural Studies by Traveling Wave Ion Mobility Spectrometry: A Critical Look at Electrospray Sources and Calibration Issues

Sun

Vahidi

Sowole

et al. 2015

J. Am. Soc. Mass Spectrom.

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Abstract. The question whether electrosprayed protein ions retain solution-like conformations continues to be a matter of debate. One way to address this issue involves comparisons of collision cross sections (Ω) measured by ion mobility spectrometry (IMS) with Ω values calculated for candidate structures. Many investigations in this area employ traveling wave IMS (TWIMS). It is often implied that nanoESI is more conducive for the retention of solution structure than regular ESI. Focusing on ubiquitin, cytochrome c, myoglobin, and hemoglobin, we demonstrate that Ω values and collisional unfolding profiles are virtually indistinguishable under both conditions. These findings suggest that gas-phase structures and ion internal energies are independent of the type of electrospray source. We also note that TWIMS calibration can be challenging because differences in the extent of collisional activation relative to drift tube reference data may lead to ambiguous peak assignments. It is demonstrated that this problem can be circumvented by employing collisionally heated calibrant ions. Overall, our data are consistent with the view that exposure of native proteins to electrospray conditions can generate kinetically trapped ions that retain solution-like structures on the millisecond time scale of TWIMS experiments.

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Section: Introductionmentioning

confidence: 99%

Protein Structural Studies by Traveling Wave Ion Mobility Spectrometry: A Critical Look at Electrospray Sources and Calibration Issues

Sun

Vahidi

Sowole

et al. 2015

J. Am. Soc. Mass Spectrom.

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“…In addition to the rapid development of other top-down native MS techniques, another recently introduced powerful tool is ion-mobility MS (IM-MS) (Allison et al, 2015;Lanucara, Holman, Gray, & Eyers, 2014;May & McLean, 2015). In this method, ionised proteins are introduced into a cell filled with inert gas.…”

Section: Membrane Protein Complexes Studied In Thin Airmentioning

confidence: 99%

Bacterial Electron Transfer Chains Primed by Proteomics

Wessels¹,

Almeida²,

Kartal³

et al. 2016

Advances in Bacterial Electron Transport Systems and Their Regulation

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Electron transport phosphorylation is the central mechanism for most prokaryotic species to harvest energy released in the respiration of their substrates as ATP. Microorganisms have evolved incredible variations on this principle, most of these we perhaps do not know, considering that only a fraction of the microbial richness is known. Besides these variations, microbial species may show substantial versatility in using respiratory systems. In connection herewith, regulatory mechanisms control the expression of these respiratory enzyme systems and their assembly at the translational and posttranslational levels, to optimally accommodate changes in the supply of their energy substrates. Here, we present an overview of methods and techniques from the field of proteomics to explore bacterial electron transfer chains and their regulation at levels ranging from the whole organism down to the Ångstrom scales of protein structures. From the survey of the literature on this subject, it is concluded that proteomics, indeed, has substantially contributed to our comprehending of bacterial respiratory mechanisms, often in elegant combinations with genetic and biochemical approaches. However, we also note that advanced proteomics offers a wealth of opportunities, which have not been exploited at all, or at best underexploited in hypothesis-driving and hypothesis-driven research on bacterial bioenergetics. Examples obtained from the related area of mitochondrial oxidative phosphorylation research, where the application of advanced proteomics is more common, may illustrate these opportunities.

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“…Still relatively new to the biomedical field, several groups have recently begun to incorporate LC-IMS-MS workflows in proteomics studies [34][35][36][37], and enhanced performance has been demonstrated [38]. Given the recent rate of growth in the IMS field [39] and its broad analytical utility, it seems prudent to expect that full maturity-both in terms of application workflows and technology performance-is yet to come.…”

Section: Introductionmentioning

confidence: 99%

Fundamentals of Trapped Ion Mobility Spectrometry Part II: Fluid Dynamics

Silveira

Michelmann

Ridgeway

et al. 2016

J. Am. Soc. Mass Spectrom.

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Abstract. Trapped ion mobility spectrometry (TIMS) is a new high resolution (R up tõ 300) separation technique that utilizes an electric field to hold ions stationary against a moving gas. Recently, an analytical model for TIMS was derived and, in part, experimentally verified. A central, but not yet fully explored, component of the model involves the fluid dynamics at work. The present study characterizes the fluid dynamics in TIMS using simulations and ion mobility experiments. Results indicate that subsonic laminar flow develops in the analyzer, with pressure-dependent gas velocities between~120 and 170 m/s measured at the position of ion elution. One of the key philosophical questions addressed is: how can mobility be measured in a dynamic system wherein the gas is expanding and its velocity is changing? We noted previously that the analytically useful work is primarily done on ions as they traverse the electric field gradient plateau in the analyzer. In the present work, we show that the position-dependent change in gas velocity on the plateau is balanced by a change in pressure and temperature, ultimately resulting in near positionindependent drag force. That the drag force, and related variables, are nearly constant allows for the use of relatively simple equations to describe TIMS behavior. Nonetheless, we derive a more comprehensive model, which accounts for the spatial dependence of the flow variables. Experimental resolving power trends were found to be in close agreement with the theoretical dependence of the drag force, thus validating another principal component of TIMS theory.

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Ion Mobility-Mass Spectrometry: Time-Dispersive Instrumentation

Cited by 364 publications

References 212 publications

Protein Structural Studies by Traveling Wave Ion Mobility Spectrometry: A Critical Look at Electrospray Sources and Calibration Issues

Protein Structural Studies by Traveling Wave Ion Mobility Spectrometry: A Critical Look at Electrospray Sources and Calibration Issues

Bacterial Electron Transfer Chains Primed by Proteomics

Fundamentals of Trapped Ion Mobility Spectrometry Part II: Fluid Dynamics

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