Billionfold data increase from mass spectrometry instrumentation

McLafferty, Fred W.

doi:10.1016/s1044-0305(96)00203-6

Cited by 14 publications

(6 citation statements)

References 51 publications

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“…Fourier transform ion cyclotron resonance mass spectrometry has been a very active area of research in mass spectrometry for over two decades. It has been the subject of several recent reviews that describe progress in the field, historical perspectives, and tutorial descriptions of the technique. − There have also been several books − and journal issues devoted to the subject. , …”

Section: Fourier Transform Ion Cyclotron Resonance Mass Spectrometrymentioning

confidence: 99%

“…It has been the subject of several recent reviews that describe progress in the field, historical perspectives, and tutorial descriptions of the technique. [101][102][103][104][105][106][107][108][109][110][111][112] There have also been several books [113][114][115] and journal issues devoted to the subject. 116,117 Modern FTICR enjoys the highest resolving power of any form of mass analysis, at least for mass-tocharge ratios less than about 10 4 , and the highest mass measurement accuracy.…”

Section: Fourier Transform Ion Cyclotron Resonance Mass Spectrometrymentioning

confidence: 99%

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Mass Analysis at the Advent of the 21st Century

2001

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There have been many new and exciting developments in mass spectrometer systems in recent years. Many of these developments are being driven by challenges presented by molecular biology. The activity is fueled by resources being devoted to drug development, for example, and other medically and biologically related activities. Progress in these applications will be accelerated by improved sensitivity, specificity, and speed. In mass spectrometry, this translates to greater mass resolving power, mass accuracy, mass-to-charge range, efficiency, and speed. It is safe to say that the demands resulting from current analytical needs are likely to be met to varying degrees but probably not by a single analyzer technology or hybrid instrument. On-line and/or off-line separations and manipulations combined with mass spectrometry will also play increasingly important roles. For any analyzer, or combination of analyzers, to become widely used it must have an important application for which its figures of merit are best suited, relative to competing approaches. The relative cost of competing technologies is also an important factor. The mass filter has seen so much use in the past 30 years because its characteristics best fit a wide range of applications. As an example, biological applications, which are currently driving many instrument development activities in mass spectrometry, demand more information, of higher quality, from less material, faster, and at lower cost. Which technologies will dominate biological applications in the coming years is open to speculation. However, in considering the relative merits of today's dominant mass analyzers, areas of opportunity for improvement are apparent. Furthermore, new and more demanding measurement needs are constantly being recognized that will continue to exercise the creativity of the mass spectrometry community.

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Section: Fourier Transform Ion Cyclotron Resonance Mass Spectrometrymentioning

confidence: 99%

Section: Fourier Transform Ion Cyclotron Resonance Mass Spectrometrymentioning

confidence: 99%

Mass Analysis at the Advent of the 21st Century

2001

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“…21,22 ESI-FTICR has proved to be remarkably powerful in structural determination of proteins, which is an activity of fundamental importance in ultimately elucidating biological function. Its contributions cannot be overstated.…”

Section: Introductionmentioning

confidence: 99%

Hydropathic influences on the quantification of equine heart cytochromec using relative ion abundance measurements by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry

et al. 1999

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“…Recent reports have described such varied investigations as highly accurate molecular mass determinations of peptides and proteins, [1][2][3][4] high resolution tandem mass spectra of exceedingly large biomolecules (b10 kDa), 2,5,6 and structural verification of 50-to 100-mer DNA and RNA sequences. 7,8 The maturation of this increasingly useful technique in the qualitative analysis of biological compounds is well documented.…”

mentioning

confidence: 99%

Quantification of singly charged biomolecules by electrospray ionization fourier transform ion cyclotron resonance mass spectrometry utilizing an internal standard

Gordon

Muddiman

1999

Rapid Commun. Mass Spectrom.

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The quantification of Cyclosporin A (CsA) and related biological compounds by various mass spectrometric techniques is well established. It is precisely this fact that makes the use of CsA particularly appealing as a model system in evaluating the quantitative properties of electrospray ionization coupled to Fourier transform ion cyclotron resonance mass spectrometry (ESI-FTICR-MS). Utilizing the internal standard methodology, we have generated a linear calibration curve ranging from 5-250 ng/mL CsA described by the equation y = 0.00503x-0.00958, with a %RSD slope of 0.74% and a correlation coefficient (r 0 ) equal to 0.999 2 (N = 30). The internal standard (200 ng/mL Cyclosporin G) was found to be necessary to establish the reported dynamic range, two orders of magnitude based on an experimentally determined detection limit of 2.4 ng/mL CsA, and also significantly improved the overall precision of the method. The data represented in the standard curve were collected as 1.05 s single acquisitions (512 K data points at an ADC rate of 500 kHz) and unapodized prior to the Fourier transformation of the time-domain data. We report that full Hanning apodization has a statistically significant negative effect (F-test at 95% confidence level) on the regression statistics of the curve (i.e. increasing the %RSD slope to 1.33%). Finally, we report that acceptable quantitative properties of an FTICR-MS experiment can be realized as soon as the detection of a second isotopic beat for the targeted species is obtained. This should allow for the practical and effective coupling of on-line separation techniques for quantitative analysis using ESI-FTICR-MS. Copyright # 1999 John Wiley & Sons, Ltd. Received 4 December 1998; Accepted 4 December 1998Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) has been demonstrated to have impressive capabilities for the analytical characterization of biological materials. Recent reports have described such varied investigations as highly accurate molecular mass determinations of peptides and proteins, 1-4 high resolution tandem mass spectra of exceedingly large biomolecules (b10 kDa), 2,5,6 and structural verification of 50-to 100-mer DNA and RNA sequences. 7,8 The maturation of this increasingly useful technique in the qualitative analysis of biological compounds is well documented. Interestingly, one area of research that has been comparatively slow to develop is the exploration of electrospray ionization (ESI) FTICR-MS as a quantitative tool. Limbach et al. reported the first experimental demonstration of the potentially achievable detection limit ($177 ions at S/N = 3) and dynamic range (b4 orders of magnitude) for an FTICR mass spectrometer with a 1.875-in cubic trap housed within a 3.0 T superconducting magnet. 9 In a more empirical approach, Padley and co-workers quantified both singly and multiply charged ions according to their absolute peak intensities 10 utilizing ESI and observed linearity of $2-3 orders of magnitude for singly charged lysine (147 Da) and 1.5 or...

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Billionfold data increase from mass spectrometry instrumentation

Cited by 14 publications

References 51 publications

Mass Analysis at the Advent of the 21st Century

Mass Analysis at the Advent of the 21st Century

Hydropathic influences on the quantification of equine heart cytochromec using relative ion abundance measurements by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry

Quantification of singly charged biomolecules by electrospray ionization fourier transform ion cyclotron resonance mass spectrometry utilizing an internal standard

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