The Role of Fourier Transform Ion Cyclotron Resonance Mass Spectrometry in Biological Research — New Developments and Applications

Smith, Richard; Bruce, James E.; Wu, Qinghao; Cheng, Xueheng; Hofstadler, Steven A.; Anderson, Gordon A.; Chen, R.; Bakhtiar, Ray; Orden, S. O. Van; Gale, David C.; Sherman, Michael G.; Rockwood, A.L.; Udseth, Harold R.

doi:10.1007/978-1-4612-0229-5_3

Cited by 6 publications

(6 citation statements)

References 76 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Additional variations on this theme of connecting two different, relatively inexpensive analyzers together to produce a more versatile instrument are under development. Although neither small or inexpensive, Fourier‐transform ion‐cyclotron resonance mass spectrometers equipped with MALDI and ESI are extremely versatile instruments with the potential for simultaneously providing very high mass accuracy, high resolution (routinely ≥20,000), and extremely high sensitivity for peptide and protein mass measurement (Winger et al, ; O'Conner et al, ; Wu et al, ; Smith et al, ). These devices are also capable of performing MS n experiments.…”

Section: Discussionmentioning

confidence: 99%

“…Mass assignment accuracies of 0.01% are routine (see Table 10.21.1 and discussion of Fundamentals of Mass Measurement Accuracy and Mass Resolution). ESI has also been successfully interfaced with ion-trap mass spectrometers (Korner et al, 1996), Fourier-transform ion-cyclotron resonance mass spectrometers (Winger et al, 1993;O'Conner et al, 1995;Wu et al, 1995;Smith et al, 1996), and TOF mass spectrometers (Mirgorodskaya et al, 1994;Verentchikov et al, 1994).…”

Section: Esi-msmentioning

confidence: 99%

“…The ability of MS to determine the molecular weights of peptides in mixtures (such as result from a proteolytic digest of a protein) with better than 0.01% accuracy forms the basis of the mass spectrometric peptide mapping strategy, a rapid and highly efficient method to verify the fidelity of translation of protein sequences deduced from DNA or cDNA sequencing. This can be done either by direct analysis of unfractionated mixtures (Billeci and Stults, 1993) or on-line with liquid chromatography (Hess et al, 1993;Carr et al, 1993;Kassel et al, 1994) or capillary electrophoresis (Wahl et al, 1992;Foret et al, 1994;Smith et al, 1996).…”

mentioning

confidence: 99%

See 2 more Smart Citations

Overview of Peptide and Protein Analysis by Mass Spectrometry

Carr

Annan

1997

CP Molecular Biology

View full text Add to dashboard Cite

The goals of this unit are to familiarize peptide and protein chemists with the types of mass spectrometers that are appropriate for the majority of their analytical needs, to describe the kinds of experiments that can be performed with these instruments on a routine basis, and to discuss the kinds of information that these experiments provide. The emphasis here is on established tools and techniques that can realistically be used for problem solving. As a result, many useful instruments and techniques employed by the trained mass spectroscopist are not discussed here, because they do not satisfy these criteria or are not yet widely available. A few of these are briefly mentioned at the end of this introductory overview. The overview concludes with a tutorial discussion on the meaning and practical importance of a number of fundamental experimental and performance-related issues that have important implications for interpretation and use of mass spectral data, such as mass accuracy and resolution.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Esi-msmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Overview of Peptide and Protein Analysis by Mass Spectrometry

Carr

Annan

1997

CP Molecular Biology

View full text Add to dashboard Cite

show abstract

“…Mass assignment accuracies of 0.01% are routine (see Table 16.1.1 and discussion of Fundamentals of Mass Measure-ment Accuracy and Mass Resolution). ESI has also been successfully interfaced with ion-trap mass spectrometers (Korner et al, 1996), Fourier-transform ion-cyclotron resonance mass spectrometers (Winger et al, 1993;O'Conner et al, 1995;Wu et al, 1995;Smith et al, 1996), and TOF mass spectrometers (Verentchikov et al, 1994;Mirgorodskaya et al, 1994).…”

Section: 111mentioning

confidence: 99%

mentioning

confidence: 99%

Overview of Peptide and Protein Analysis by Mass Spectrometry

Carr

Annan

1996

CP Protein Science

View full text Add to dashboard Cite

One goal of this introductory overview is to try and dispel the still widely held, but now mistaken, belief that mass spectrometry is beyond the technical resources of the typical laboratory or facility engaged in the structural characterization or synthesis of peptides and proteins. Over the last five years, mass spectrometers and associated data systems have become available that can be operated by anyone capable of running a modern amino acid analyzer or Edman sequencer, yet are powerful enough to handle the most demanding analyses that the peptide or protein investigator might require. The remaining goals of this article are to familiarize peptide and protein chemists with the types of mass spectrometers that are appropriate for the majority of their analytical needs, to describe the kinds of experiments that can be performed with these instruments on a routine basis, and to discuss the kinds of information that these experiments provide. The emphasis here is on established tools and techniques that can realistically be used for problem solving. As a result, many useful instruments and techniques employed by the trained mass spectroscopist are not discussed here, because they do not satisfy these criteria or are not yet widely available; however, a few of these are briefly mentioned at the end of the unit. The overview concludes with a tutorial discussion on the meaning and practical importance of a number of fundamental experimental and performance-related issues that have important implications for interpretation and use of mass spectral data, such as mass accuracy and resolution.

show abstract

Combined Analyzer Technologies

Kofel

Schlunegger

1997

Selected Topics in Mass Spectrometry in the Biomolecular Sciences

View full text Add to dashboard Cite

The Role of Fourier Transform Ion Cyclotron Resonance Mass Spectrometry in Biological Research — New Developments and Applications

Cited by 6 publications

References 76 publications

Overview of Peptide and Protein Analysis by Mass Spectrometry

Overview of Peptide and Protein Analysis by Mass Spectrometry

Overview of Peptide and Protein Analysis by Mass Spectrometry

Combined Analyzer Technologies

Contact Info

Product

Resources

About