Proteomics in 2002:  A Year of Technical Development and Wide-Ranging Applications

Figeys, Daniel

doi:10.1021/ac030142m

Cited by 89 publications

(73 citation statements)

References 195 publications

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“…As shown in Figure 5, a plot of K 0 vs. E 0 /p, this observation is also consistent with other IMS measurements on a wide range of analytes including atomic, small organic, and fullerene ions [37,38]. The representative data for the additional classes of ions shown in Figure 5 (Ar ϩ for the atomic ions, CH 3 CHOH ϩ for small organic ions, C 60 ϩ for fullerene ions, and NTDGSTDYGILQINSR for the [M ϩ H] ϩ tryptic peptide ions) were all acquired under conditions that minimize the influence of gas-phase chemistry on the mobility separation (i.e., low pressure, high gas purity, low relative humidity) and thus emphasizing the influence of ion transport at high field strengths on the separation, with the effect of high field diffusion more pronounced for the higher mobility species. Overall, the tryptic peptide data presented here is completely consistent with eq 2 and the literature data presented in Figure 5, indicating that the effects of drift cell reaction chemistry on the tryptic peptide separation are minimized.…”

supporting

confidence: 89%

“…Atomic data for Ar ϩ from reference and small organic data for CH 3 CHOH ϩ from reference [36], fullerene data for C 60 ϩ from reference [37], and tryptic peptide data for NTDGSTDYGILQINSR [M ϩ H] ϩ ion from this work.…”

Section: Discussionmentioning

confidence: 99%

“…For example, several groups have used liquid chromatography-mass spectrometry (LC-MS) for identification of components of simple proteomes, and have reported enhanced sequence coverage, limit-of-detection, dynamic range, and peak capacity relative to MS-only methods of analysis [1,2]. Prior to the development of LC-MS techniques for proteomics, mass spectrometry of 2-D gel-separated proteins was the method of choice for large-scale protein identification, because the method provides both excellent peak capacity and modestly improved dynamic range [3,4]. However, both LC and 2-D gel separations inefficiently utilize MS detection, because separations can take 5 to 10 orders of magnitude longer than necessary for mass spectrometry detection (i.e., Ͻ100 s for time-of-flight (TOF) MS) [5].…”

mentioning

confidence: 99%

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The influence and utility of varying field strength for the separation of tryptic peptides by ion mobility-mass spectrometry

Ruotolo

McLean

Gillig

et al. 2005

J. Am. Soc. Mass Spectrom.

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The influence of field strength on the separation of tryptic peptides by drift tube-based ion mobility-mass spectrometry is reported. Operating the ion mobility drift tube at elevated field strengths (expressed in V cm Ϫ1 torr Ϫ1 ) reduces separation times and increases ion transmission efficiencies. Several accounts in the literature suggest that performing ion mobility separation at elevated field strength can change the selectivity of ion separation. To evaluate the field strength dependant selectivity of ion mobility separation, we examined a data set of 65 singly charged tryptic peptide ion signals (mass range 500 -2500 m/z) at six different field strengths and four different drift gas compositions (He, N 2 , Ar, and CH 4 ). Our results clearly illustrate that changing the field strength from low field (15 V cm Ϫ1 torr Ϫ1) to high field (66 V cm Ϫ1 torr Ϫ1 ) does not significantly alter the selectivity or peak capacity of IM-MS. The implications of these results are discussed in the context of separation methodologies that rely on the field strength dependence of ion mobility for separation selectivity, e.g., high-field asymmetric ion mobility spectrometry ( H ybrid mass spectrometry techniques have emerged as powerful tools for complex mixture analysis. For example, several groups have used liquid chromatography-mass spectrometry (LC-MS) for identification of components of simple proteomes, and have reported enhanced sequence coverage, limit-of-detection, dynamic range, and peak capacity relative to MS-only methods of analysis [1,2]. Prior to the development of LC-MS techniques for proteomics, mass spectrometry of 2-D gel-separated proteins was the method of choice for large-scale protein identification, because the method provides both excellent peak capacity and modestly improved dynamic range [3,4]. However, both LC and 2-D gel separations inefficiently utilize MS detection, because separations can take 5 to 10 orders of magnitude longer than necessary for mass spectrometry detection (i.e., Ͻ100 s for time-of-flight (TOF) MS) [5].Ion mobility (IM) separation (based on ion collision cross-section) coupled with mass spectrometry possesses many of the same advantages of LC-MS approaches, i.e., enhanced dynamic range and increased peak capacity when compared with MS-only analysis [6,7]. Further, IM separations require only milliseconds (typically 500 s to 2 ms for tryptic peptides), which is better suited to MS timescales [8]. For example, both Russell (using matrix assisted laser desorption ionization -MALDI) and Clemmer (using electrospray ionization -ESI) have utilized IM-MS for the analysis of complex protein mixtures [9,10]. In the case of MALDI-IM-MS protein mixture analysis, the hybrid separation technique provided enhanced percent amino acid sequence coverage through the increased dynamic range relative to MS-only analysis [9]. Clemmer and coworkers used LC-ESI-IM-MS to analyze biologically derived complex mixtures, and demonstrated that the combination of LC and IM provides complementary separation...

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supporting

confidence: 89%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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The influence and utility of varying field strength for the separation of tryptic peptides by ion mobility-mass spectrometry

Ruotolo

McLean

Gillig

et al. 2005

J. Am. Soc. Mass Spectrom.

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“…13,14 The studies that analyze vast amounts of samples and compounds silica monolithic column has some advantages over the such as metabolomics and proteomics. [1][2][3][4] In order to accomplish polymer-based one, e.g. well controlled pore structure, good high speed separation on high performance liquid chromatography mechanical strength, and high column efficiency especially for (HPLC), one must solve two problems at high flow rate: small molecules.…”

Section: Introductionmentioning

confidence: 99%

Methacrylate-ester-based Reversed Phase Monolithic Columns for High Speed Separation Prepared by Low Temperature UV Photo-polymerization

2009

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Butyl methacrylate-based reversed phase capillary monolithic columns were prepared using ultraviolet (UV) photo-polymerization. The effects of two photo-polymerization conditions (UV irradiation intensity and polymerization temperature) on the column characteristics were investigated. Both the higher UV irradiation intensity and the lower polymerization temperature lead to the superior column efficiency. The column prepared under the optimized conditions was evaluated through the separation of the uracil and five alkylbenzenes in the linear flow rate range of 1 -110 mm/s. At 1 mm/s, all analytes were well separated (N = 36000 -45000 plates/m). The high speed separation within 8 s was performed at 110 mm/s (back pressure, 33 MPa) at room temperature, whereas the peaks eluted earlier were overlapped partially. The relationship between the flow rate and the back pressure indicated that some kind of structural change of the monolith might occur in 50 -110 mm/s, although no visible or hysteresis changes of the monolith were observed after the measurement.

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“…[1][2][3][4][5][6][7][8][9][10][11][12][13][14] By building on these and earlier efforts, it is anticipated that the popularity of CE-MS will grow, and its advantages will be better appreciated and exploited.…”

Section: Introductionmentioning

confidence: 99%

Recent Developments in Capillary Electrophoresis–Mass Spectrometry of Proteins and Peptides

Monton

Terabe

2005

ANAL. SCI.

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Many researchers have invested considerable efforts toward improving capillary electrophoresis (CE)-mass spectrometry (MS) systems so they can be applied better to standard analyses. This review highlights the developments in CE-MS of proteins and peptides over the last five years. It includes the developments in interfaces, sample-enrichment techniques, microfabricated devices, and some applications, largely in capillary zone electrophoresis (CZE), capillary isoelectric focusing (CIEF) and capillary isotachophoresis formats.

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Proteomics in 2002: A Year of Technical Development and Wide-Ranging Applications

Cited by 89 publications

References 195 publications

The influence and utility of varying field strength for the separation of tryptic peptides by ion mobility-mass spectrometry

The influence and utility of varying field strength for the separation of tryptic peptides by ion mobility-mass spectrometry

Methacrylate-ester-based Reversed Phase Monolithic Columns for High Speed Separation Prepared by Low Temperature UV Photo-polymerization

Recent Developments in Capillary Electrophoresis–Mass Spectrometry of Proteins and Peptides

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