Exact mass measurements using a 7 tesla fourier transform ion cyclotron resonance mass spectrometer in a good laboratory practices-regulated environment

Burton, Richard D. E.; Matuszak, Kenneth P.; Watson, Clifford H.; Eyler, John R.

doi:10.1016/s1044-0305(99)00106-3

Cited by 47 publications

(65 citation statements)

References 24 publications

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“…The ion signal was digitized at a 761,904 Hz acquisition frequency for 688 ms (512 Kb data points). The resulting transient was zero-filled twice before Fourier transformation and the peaks were picked in the frequency domain using a 3 points quadratic approximation which was previously shown to provide the best MMA [10]. Only monoisotopic peaks with signal to noise Ͼ3 and relative intensity Ͼ5% were used to generate the calibration.…”

Section: Methodsmentioning

confidence: 99%

“…When online separations are used, the analyte ion production rates vary widely, and the ion population in the trap cannot be easily or precisely controlled. Although mass accuracies in the sub-ppm level have been reported using internal calibration [10], external calibration typically doesn't provide accuracies better than several ppm, unless the ion population (and achievable dynamic range) is severely constrained, or when the ion population for the measurement differs significantly from the ion population used for the calibration [9]. In FTICR, the highest MMA have been obtained with small ion populations, often with the use of summation (or signal averaging) of many spectra and with the application of internal calibration.…”

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confidence: 99%

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Mass measurement errors caused by “local” frequency perturbations in FTICR mass spectrometry

Masselon

Tolmachev

Anderson

et al. 2002

J. Am. Soc. Mass Spectrom.

102

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One of the key qualities of mass spectrometric measurements for biomolecules is the mass measurement accuracy (MMA) obtained. FTICR presently provides the highest MMA over a broad m/z range. However, due to space charge effects, the achievable MMA crucially depends on the number of ions trapped in the ICR cell for a measurement. Thus, beyond some point, as the effective sensitivity and dynamic range of a measurement increase, MMA tends to decrease. While analyzing deviations from the commonly used calibration law in FTICR we have found systematic errors which are not accounted for by a "global" space charge correction approach. The analysis of these errors and their dependence on charge population and post-excite radius have led us to conclude that each ion cloud experiences a different interaction with other ion clouds. We propose a novel calibration function which is shown to provide an improvement in MMA for all the spectra studied. (J Am Soc Mass Spectrom 2002, 13, 99 -106)

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Mass measurement errors caused by “local” frequency perturbations in FTICR mass spectrometry

Masselon

Tolmachev

Anderson

et al. 2002

J. Am. Soc. Mass Spectrom.

102

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“…The GC/FT-ICR MS utilizes the separation capability of a conventional GC [12] as well as mass measurement accuracy [8,9,13,14] and superior mass resolving power of FT-ICR MS [15,16]. The advantages of multidimensional and/or "hyphenated" chromatography techniques with spectroscopic detectors were reviewed extensively [17].…”

mentioning

confidence: 99%

A preconcentrator coupled to a GC/FTMS: Advantages of self-chemical ionization, mass measurement accuracy, and high mass resolving power for GC applications

Solouki

Szulejko

Bennett

et al. 2004

J. Am. Soc. Mass Spectrom.

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“…Each spectrum was baseline corrected, Hanning apodized [44] and zerofilled twice. The thorough high resolution analysis of spectra by Horn (THRASH) program was used to generate the experimental peak lists obtained for the ECD experiments [45].…”

Section: Discussionmentioning

confidence: 99%

Identification of single and double sites of phosphorylation by ECD FT-ICR/MS in peptides related to the phosphorylation site domain of the myristoylated alanine-rich c kinase protein

Woodling

Eyler

Tsybin

et al. 2007

J. Am. Soc. Mass Spectrom.

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A series of phosphorylated test peptides was studied by electron capture dissociation Fourier transform ion cyclotron resonance mass spectrometry (ECD FT-ICR MS). The extensive ECD-induced fragmentation made identification of phosphorylation sites for these peptides straightforward. The site(s) of initial phosphorylation of a synthetic peptide with a sequence identical to that of the phosphorylation site domain (PSD) of the myristoylated alanine-rich C kinase (MARCKS) protein was then determined. Despite success in analyzing fragmentation of the smaller test peptides, a unique site on the PSD for the first step of phosphorylation could not be identified because the phosphorylation reaction produced a heterogeneous mixture of products. Some molecules were phosphorylated on the serine closest to the N-terminus, and others on one of the two serines closest to the C-terminus of the peptide. Although no definitive evidence for phosphorylation on either of the remaining two serines in the PSD was found, modification there could not be ruled out by the ECD fragmentation data. . This protein also binds calmodulin [7], acidic membrane phospholipids [8 -10], and actin filaments [11]. These interactions are believed to be regulated by protein phosphorylation [3,4,12,13]. The MARCKS protein is also a major substrate for protein kinase C (PKC) [14]. Protein kinase C-related kinase (PRK1) and -associated kinase also phosphorylate the phosphorylation site domain (PSD) [15,16]. PKC contains two regions: the N-terminal regulatory region and the C-terminal catalytic region. This kinase phosphorylates serine and threonine residues in basic peptide and protein sequences. Thus, PKC phosphorylates a small segment of the MARCKS protein, displacing the protein from membranes. The phosphorylation of the MARCKS protein then inhibits cross-linking activity of filamentous (F) actin, calcium-calmodulin binding, and binding to the plasma membrane [3,7,9,11,[17][18][19].The MARCKS protein contains three highly conserved regions: the phosphorylation site domain (PSD), the myristoylated amino-terminal domain, and the MARCKS homology domain. The PSD region, also known as the effector domain (ED), is the most studied, and is a basic peptide comprised of 25 amino acid residues. This region is believed to be central to the activity of the MARCKS protein.

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Exact mass measurements using a 7 tesla fourier transform ion cyclotron resonance mass spectrometer in a good laboratory practices-regulated environment

Cited by 47 publications

References 24 publications

Mass measurement errors caused by “local” frequency perturbations in FTICR mass spectrometry

Mass measurement errors caused by “local” frequency perturbations in FTICR mass spectrometry

A preconcentrator coupled to a GC/FTMS: Advantages of self-chemical ionization, mass measurement accuracy, and high mass resolving power for GC applications

Identification of single and double sites of phosphorylation by ECD FT-ICR/MS in peptides related to the phosphorylation site domain of the myristoylated alanine-rich c kinase protein

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