The Early Development of Fourier Transform Ion Cyclotron Resonance FTICR Spectroscopy

Comisarow, Melvin B.; Marshall, Alan

doi:10.1002/(sici)1096-9888(199606)31:6<581::aid-jms369>3.3.co;2-t

Cited by 11 publications

(13 citation statements)

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“…By the same mechanism the formation of other internal b ions can be rationalized accordingly. The prevailance of this mechanism effects that near the N-terminus the internal dipeptide ions b i (3)(4) and b i(5-6) are preferentially formed. However, as evident from Fig.…”

Section: Mechanism Of Formation Of Internal B Ionsmentioning

confidence: 99%

“…In the meantime, the introduction of Fourier transform ion cyclotron resonance MS [3], delayed-extraction MALDI-TOF [4][5], and of quadrupole-time of flight tandem mass spectrometry (Q-TOF) analyzers [6,7] allows the registration of survey and MS/MS spectra both in ESI and MALDI mode at resolution of about 10 000 or more, with concomitant increase in mass measurement accuracy to 10 ppm or better. The confidence of protein identification by the mass fingerprinting approach is highly improved by accurate mass measurement of the peptide molecular weights [8,9].…”

Section: Introductionmentioning

confidence: 99%

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Patchwork peptide sequencing: Extraction of sequence information from accurate mass data of peptide tandem mass spectra recorded at high resolution*

Schlösser

Lehmann

2002

Proteomics

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The accurate mass values of all immonium, y(1), y(2), a(2), and b(2) ions of tryptic peptides composed of the 20 standard amino acids were calculated. The differences between adjacent masses in this data set are greater than 10 mDa for more than 80% of the values. Using this mass list, the majority of low mass ions in quadrupole-time of flight tandem mass spectra of peptides from tryptic digests and from an elastase digest could be assigned. Besides the a(2)/b(2) ions, which carry residues 1-2 from the N-terminus, a variety of internal dipeptide b ions were regularly observed. In case internal proline was present, corresponding dipeptide b ions carrying proline at the N-terminal position occurred. By assigning the dipeptide b ions on the basis of their accurate mass, bidirectional or unidirectional sequence information was obtained, which is localized to the peptide N-terminus (a(2)/b(2) ions) or not localized (internal b ions). Identification of the y(1) and y(2) ions by their accurate mass provides unidirectional sequence information localized to the peptide C-terminus. It is shown that this patchwork-type sequence information extractable from accurate mass data of low-mass ions is highly efficient for protein identification.

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Section: Mechanism Of Formation Of Internal B Ionsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Patchwork peptide sequencing: Extraction of sequence information from accurate mass data of peptide tandem mass spectra recorded at high resolution*

Schlösser

Lehmann

2002

Proteomics

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“…The first is the Fourier transform ion cyclotron resonance mass spectrometer (FT-ICR). 35 The second is the Orbitrap, which also uses an FT-based strategy. 36 For example, Mann and co-workers 27 have used an FT-ICR to identify sequence-specific DNA-binding proteins in HeLa S3 cells purified by DNA affinity chromatography.…”

Section: Mass Spectrometrymentioning

confidence: 99%

DNA-centered approaches to characterize regulatory protein–DNA interaction complexes

Simicevic

Deplancke

2010

Mol. BioSyst.

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Gene regulation is mediated by site-specific DNA-binding proteins or transcription factors (TFs), which form protein complexes at regulatory loci either to activate or repress the expression of a target gene. The study of the dynamic properties of these regulatory DNA-binding complexes has so far been dominated by protein-centered methodologies, aiming to characterize the DNA-binding behavior of one specific protein at a time. With the emerging evidence for a role of DNA in allosterically influencing DNA-binding protein complex formation, there is renewed interest in DNA-centered approaches to capture protein complexes on defined regulatory loci and to correlate changes in their composition with alterations in target gene expression. In this review, we present the current state-of-the-art in such DNA-centered approaches and evaluate recent technological improvements in the purification as well as in the identification of regulatory DNA-binding protein complexes within or outside their biological context. Finally, we suggest possible areas of improvement and assess the putative impact of DNA-centered methodologies on the gene regulation field for the forthcoming years.

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“…In 1974, Comisarow and Marshall significantly improved ICR mass spectrometry by building the first Fourier transform ion cyclotron resonance (FTICR) mass spectrometer [39], analogously to previous FT spectroscopies, particularly FTNMR [40,41]. Marshall, Comisarow and others have since continuously improved FTICR mass spectrometry, increasing the mass range, mass resolving power and sensitivity of the technique [42,43].…”

Section: Figurementioning

confidence: 99%

Identification and Characterization of Peptides and Proteins Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Palmblad

Bergquist

2003

Journal of Chromatography Library

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Mass spectrometry has in recent years been established as the standard method for protein identification and characterization in proteomics with excellent intrinsic sensitivity and specificity. Fourier transform ion cyclotron resonance is the mass spectrometric technique that provides the highest resolving power and mass accuracy, increasing the amount of information that can be obtained from complex samples. This thesis concerns how useful information on proteins of interest can be extracted from mass spectrometric data on different levels of protein structure and how to obtain this data experimentally. It was shown that it is possible to analyze complex mixtures of protein tryptic digests by direct infusion electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry and identify abundant proteins by peptide mass fingerprinting. Coupling on-line methods such as liquid chromatography and capillary electrophoresis increased the number of proteins that could be identified in human body fluids. Protein identification was also improved by novel statistical methods utilizing prediction of chromatographic behavior and the non-randomness of enzymatic digestion. To identify proteins by short sequence tags, electron capture dissociation was implemented, improved and finally coupled on-line to liquid chromatography for the first time. The combined techniques can be used to sequence large proteins de novo or to localize and characterize any labile post-translational modification. New computer algorithms for the automated analysis of isotope exchange mass spectra were developed to facilitate the study of protein structural dynamics. The non-covalent interaction between HIV-inhibitory peptides and the oligomerization of amyloid β-peptides were investigated, reporting several new findings with possible relevance for development of anti-HIV drug therapies and understanding of fundamental mechanisms in Alzheimer's disease.

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The Early Development of Fourier Transform Ion Cyclotron Resonance FTICR Spectroscopy

Cited by 11 publications

References 0 publications

Patchwork peptide sequencing: Extraction of sequence information from accurate mass data of peptide tandem mass spectra recorded at high resolution*

Patchwork peptide sequencing: Extraction of sequence information from accurate mass data of peptide tandem mass spectra recorded at high resolution*

DNA-centered approaches to characterize regulatory protein–DNA interaction complexes

Identification and Characterization of Peptides and Proteins Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

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