Collision-Induced Dissociation of Mobility-Separated Ions Using an Orifice-Skimmer Cone at the Back of a Drift Tube

Lee, Young Jin; Hoaglund-Hyzer, Cherokee S.; Taraszka, John A.; Zientara, Gina A.; Counterman, and Anne E.; Clemmer, David E.

doi:10.1021/ac010295e

Cited by 40 publications

(37 citation statements)

References 18 publications

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“…This field is created by applying voltages to three electrodes near the exit of the drift tube: the last drift tube lens with grid (90% transmittance, Ni) of the first field region of the drift tube; an inverted stainless steel conical lens; and, the exit orifice plate that is constructed of BeCu. Overall, these electrodes are designed to create a balloonshaped field for focusing the diffuse ion cloud through the BeCu exit hole [41]; at high-fields, the region also can be used to induce dissociation [40]. Also shown in Figure 2 are two example plots of the equipotential lines (obtained from modeling the system of electrodes using the SIMION program) [42] for the exit region of the drift tube that represents typical conditions that we have employed in these studies.…”

Section: A Split-field Drift Tube For Ion Separation and Collisional mentioning

confidence: 99%

Nanoflow LC/IMS-MS and LC/IMS-CID/MS of protein mixtures

Sowell

Koeniger

Valentine

et al. 2004

J. Am. Soc. Mass Spectrom.

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A simple ion trap/ion mobility/time-of-flight (TOF) mass spectrometer has been coupled with nanoflow liquid chromatography to examine the feasibility of analyzing mixtures of intact proteins. In this approach proteins are separated using reversed-phase chromatography. As components elute from the column, they are electrosprayed into the gas phase and separated again in a drift tube prior to being dispersed and analyzed in a TOF mass spectrometer. The mobilities of ions through a buffer gas depend upon their collision cross sections and charge states; separation based on these gas-phase parameters provides a new means of simplifying mass spectra and characterizing mixtures. Additionally it is possible to induce dissociation at the exit of the drift tube and examine the fragmentation patterns of specific protein ion charge states and conformations. The approach is demonstrated by examining a simple threecomponent mixture containing ubiquitin, cytochrome c, and myoglobin and several larger prepared protein mixtures. The potential of this approach for use in proteomic applications is considered. (J Am Soc Mass Spectrom 2004, 15, 1341-1353

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Section: A Split-field Drift Tube For Ion Separation and Collisional mentioning

confidence: 99%

Nanoflow LC/IMS-MS and LC/IMS-CID/MS of protein mixtures

Sowell

Koeniger

Valentine

et al. 2004

J. Am. Soc. Mass Spectrom.

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“…Importantly, no ion losses caused by ion dispersion in the drift tube and in the TOF MS interface region are considered in the above analysis for the signal averaging IMS approach. Though drastically minimized due to high-field focusing elements at the drift tube exit 15 and the ion funnel interface, 16 the transmission losses between the IMS ion gate and TOF MS further deteriorate the instrument detection limit.…”

Section: Introductionmentioning

confidence: 99%

Dynamically Multiplexed Ion Mobility Time-of-Flight Mass Spectrometry

et al. 2008

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Ion Mobility Spectrometry-Time-of-Flight Mass Spectrometry (IMS-TOFMS) has been increasingly used in analysis of complex biological samples. A major challenge is to transform IMS-TOFMS to a high-sensitivity high-throughput platform for e.g. proteomics applications. In this work, we have developed and integrated three advanced technologies, including efficient ion accumulation in the ion funnel trap prior to IMS separation, multiplexing (MP) of ion packet introduction into the IMS drift tube and signal detection with an analog-to-digital converter (ADC), into the IMS-TOFMS system for the high-throughput analysis of highly complex proteolytic digests of e.g. blood plasma. To better address variable sample complexity, we have developed and rigorously evaluated a novel dynamic MP approach that ensures correlation of the analyzer performance with an ion source function, and provides the improved dynamic range and sensitivity throughout the experiment. The MP IMS-TOF MS instrument has been shown to reliably detect peptides at a concentration of 1 nM in the presence of highly complex matrix, as well as to provide a three orders of magnitude dynamic range and a mass measurement accuracy of better than 5 ppm. When matched against human blood plasma database, the detected IMS-TOF features were found to yield ~ 700 unique peptide identifications at a false discovery rate (FDR) of ~ 7.5 %. Accounting for IMS information gave rise to a projected FDR of ~ 4 %. Signal reproducibility was found to be greater than 80 %, while the variations in the number of unique peptide identifications were < 15 %. A single sample analysis was completed in 15 min that constitutes almost an order of magnitude improvement compared to a more conventional LC-MS approach.

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“…CID is also readily adapted to IMS experiments owing to the presence of a buffer gas at elevated pressures in the IMS cell. Clemmer and coworkers have demonstrated two approaches to CID fragmentation of ions as they exit the mobility cell: (1) by applying a high electric field between the drift tube and mass analyzer [10], and (2) a split-field drift cell design [14]. Additionally, Waters Corporation has introduced an rf ion guide as an interface for their traveling-wave mobility cell that is CID capable [15,16].…”

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confidence: 99%

“…That is, the ion mobility spectrometry (IMS) separation provides a temporal correlation between the precursor and product ions, circumventing the need to pre-select each precursor mass of interest [1,9,10]. A number of fragmentation techniques have been previously developed with IM-MS; including photodissociation [11], surface-induced dissociation (SID) [12,13], and collision-induced dissociation (CID) [10,14].…”

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confidence: 99%

A novel approach to collision-induced dissociation (CID) for ion mobility-mass spectrometry experiments

Becker

Fernandez-Lima

Gillig

et al. 2009

J. Am. Soc. Mass Spectrom.

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Collision induced dissociation (CID) combined with matrix assisted laser desorption ionizationion mobility-mass spectrometry (MALDI-IM-MS) is described. In this approach, peptide ions are separated on the basis of mobility in a 15 cm drift cell. Following mobility separation, the ions exit the drift cell and enter a 5 cm vacuum interface with a high field region (up to 1000 V/cm) to undergo collisional activation. Ion transmission and ion kinetic energies in the interface are theoretically evaluated accounting for the pressure gradient, interface dimensions, and electric fields. Using this CID technique, we have successfully fragmented and sequenced a number of model peptide ions as well as peptide ions obtained by a tryptic digest. This instrument configuration allows for the simultaneous determination of peptide mass, peptide-ion sequence, and collision-cross section of MALDI-generated ions, providing information critical to the identification of unknown components in complex proteomic samples. ncorporation of post-ionization, gas-phase separations with matrix assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) represents a significant advance in bioanalytical research, especially studies of proteomics [1,2] and imaging mass spectrometry [3,4]. Ion mobility-mass spectrometry (IM-MS) offers several advantages over traditional MS, including increased dynamic range [5], discrimination against chemical noise [5,6], the ability to separate geometric isomers [7], and separation of ions based on composition and charge state [1,8]. The cumulative result is highly sensitive, information-rich datasets that are unique to IM-MS techniques. For example, a single IM-MS separation can provide peptide molecular weights (peptide mass-fingerprint), ion-neutral collision cross-sections, and residue specific identification of post-translational modifications (PTMs) [1,2].When coupled to fragment ion analysis for determination of primary structure, IM-MS adds a "per sample" throughput advantage over traditional MALDI-MS/MS techniques. That is, the ion mobility spectrometry (IMS) separation provides a temporal correlation between the precursor and product ions, circumventing the need to pre-select each precursor mass of interest [1,9,10]. A number of fragmentation techniques have been previously developed with IM-MS; including photodissociation [11], surface-induced dissociation (SID) [12,13], and collision-induced dissociation (CID) [10,14]. Among the available fragmentation techniques, CID is the most widely used owing to the robust nature of the experiment and the high level of sequence coverage obtained. CID is also readily adapted to IMS experiments owing to the presence of a buffer gas at elevated pressures in the IMS cell. Clemmer and coworkers have demonstrated two approaches to CID fragmentation of ions as they exit the mobility cell: (1) by applying a high electric field between the drift tube and mass analyzer [10], and (2) a split-field drift cell design [14]. Additionally, Waters Corpora...

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Collision-Induced Dissociation of Mobility-Separated Ions Using an Orifice-Skimmer Cone at the Back of a Drift Tube

Cited by 40 publications

References 18 publications

Nanoflow LC/IMS-MS and LC/IMS-CID/MS of protein mixtures

Nanoflow LC/IMS-MS and LC/IMS-CID/MS of protein mixtures

Dynamically Multiplexed Ion Mobility Time-of-Flight Mass Spectrometry

A novel approach to collision-induced dissociation (CID) for ion mobility-mass spectrometry experiments

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