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Transform Ion Cyclotron Resonance Mass Spectrometer (transform + ion_cyclotron_resonance_mass_spectrometer)
Kinds of Transform Ion Cyclotron Resonance Mass Spectrometer Selected AbstractsOrganization of nucleobase-functionalized ,-peptides investigated by soft electrospray ionization mass spectrometryJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 5 2009Nicola Diezemann Abstract The development and validation of analytical methods is a key to succeed in investigating noncovalent interactions between biomolecules or between small molecules and biomolecules. Electrospray ionization mass spectrometry (ESI-MS) was applied with a Fourier transform ion cyclotron resonance mass spectrometer (FTICR-MS) as well as a quadrupole/time-of-flight tandem mass spectrometer (QqToF-MS) for a systematic investigation of noncovalent complexes based on nucleobase pairing in an artificial and noncharged backbone topology. Synthetical ,-peptide helices covalently modified with nucleobases were organized by recognition of a sequence of four nucleobases. Specific duplexes of ,-peptide helices were obtained on the basis of hydrogen bonding base pair complementarity. Oligomer interactions were detected with defined stoichiometry and sensitivity for the respective duplex stability. FTICR-MS and QqToF-MS were used equally well to indicate double strand stabilities in agreement with the dissociation data determined by UV spectroscopy. Furthermore, the dissociation energies of gas phase ions of the noncovalent complexes were analyzed with collision induced dissociation (CID)-MS/MS and infrared multiphoton dissociation (IRMPD)-MS/MS. The CID conditions turned out to be too harsh for a differentiation of the duplex stabilities, whereas IRMPD might be developed as a technique to detect even small interaction energy differences. Copyright © 2009 John Wiley & Sons, Ltd. [source] Gas-phase basicities for ions from bradykinin and its des-arginine analoguesJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 8 2001Nigel P. Ewing Abstract Apparent gas-phase basicities (GBapps) for [M + H]+ of bradykinin, des-Arg1 -bradykinin and des-Arg9 -bradykinin have been assigned by deprotonation reactions of [M + 2H]2+ in a Fourier transform ion cyclotron resonance mass spectrometer. With a GBapp of 225.8 ± 4.2 kcal mol,1, bradykinin [M + H]+ is the most basic of the ions studied. Ions from des-Arg1 -bradykinin and des-Arg9 -bradykinin have GBapp values of 222.8 ± 4.3 kcal mol,1 and 214.9 ± 2.3 kcal mol,1, respectively. One purpose of this work was to determine a suitable reaction efficiency ,break point' for assigning GBapp values to peptide ions using the bracketing method. An efficiency value of 0.1 (i.e. approximately 10% of all collisions resulting in a deprotonation reaction) was used to assign GBapps. Support for this criterion is provided by the fact that our GBapp values for des-Arg1 -bradykinin and des-Arg9 -bradykinin are identical, within experimental error, to literature values obtained using a modified kinetic method. However, the GBapps for bradykinin ions from the two studies differ by 10.3 kcal mol,1. The reason for this is not clear, but may involve conformation differences produced by experimental conditions. The results may be influenced by salt-bridge conformers and/or by conformational changes caused by the use of a proton-bound heterodimer in the kinetic method. Factors affecting the basicities of these peptide ions are also discussed, and molecular modeling is used to provide information on protonation sites and conformations. The presence of two highly basic arginine residues on bradykinin results in its high GBapp, while the basicity of des-Arg1 -bradykinin ions is increased by the presence of two proline residues at the N-terminus. The proline residue in the second position folds the peptide chain in a manner that increases intramolecular hydrogen bonding to the protonated N-terminal amino group of the proline at the first position. Copyright © 2001 John Wiley & Sons, Ltd. [source] Protein identification in cerebrospinal fluid using packed capillary liquid chromatography Fourier transform ion cyclotron resonance mass spectrometryPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 2 2003Margareta Ramström Abstract The identification and characterization of proteins in complex biological samples such as body fluids, require powerful and reliable tools. Mass spectrometry is today one of the most important methods in such research. This paper reports on the results from the first experiment where a tryptic digest of cerebrospinal fluid was analyzed applying reversed phase liquid chromatography coupled on-line to a 9.4 T Fourier transform ion cyclotron resonance mass spectrometer. In total, 70,204 peaks were detected, which originated from 16,296 isotopic clusters corresponding to 6551 unique peptide masses. From these masses, 39 proteins were identified in the sample. The amount of sample required for one experiment corresponds to 32 ,L of cerebrospinal fluid. [source] Towards a universal product ion mass spectral library , reproducibility of product ion spectra across eleven different mass spectrometersRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 12 2008Chris Hopley Product ion spectra produced by collision-induced dissociation (CID) in tandem mass spectrometry experiments can differ markedly between instruments. There have been a number of attempts to standardise the production of product ion spectra; however, a consensus on the most appropriate approach to the reproducible production of spectra has yet to be reached. We have previously reported the comparison of product ion spectra on a number of different types of instruments , a triple quadrupole, two ion traps and a Fourier transform ion cyclotron resonance mass spectrometer (Bristow AWT, Webb KS, Lubben AT, Halket JM. Rapid Commun. Mass Spectrom. 2004; 18: 1). The study showed that a high degree of reproducibility was achievable. The goal of this study was to improve the comparability and reproducibility of CID product ion mass spectra produced in different laboratories and using different instruments. This was carried out experimentally by defining a spectral calibration point on each mass spectrometer for product ion formation. The long-term goal is the development of a universal (instrument independent) product ion mass spectral library for the identification of unknowns. The spectra of 48 compounds have been recorded on eleven mass spectrometers: six ion traps, two triple quadrupoles, a hybrid triple quadrupole, and two quadrupole time-of-flight instruments. Initially, 4371 spectral comparisons were carried out using the data from eleven instruments and the degree of reproducibility was evaluated. A blind trial has also been carried out to assess the reproducibility of spectra obtained during LC/MS/MS. The results suggest a degree of reproducibility across all instrument types using the tuning point technique. The reproducibility of the product ion spectra is increased when comparing the tandem in time type instruments and the tandem in space instruments as two separate groups. This may allow the production of a more limited, yet useful, screening library for LC/MS/MS identification using instruments of the same type from different manufacturers. Copyright © 2008 John Wiley & Sons, Ltd. [source] Electron transfer dissociation in the hexapole collision cell of a hybrid quadrupole-hexapole Fourier transform ion cyclotron resonance mass spectrometerRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 3 2008Desmond A. Kaplan Electron transfer dissociation (ETD) of proteins is demonstrated in a hybrid quadrupole-hexapole Fourier transform ion cyclotron resonance mass spectrometer (Qh-FTICRMS). Analyte ions are selected in the mass analyzing quadrupole, accumulated in the hexapole linear ion trap, reacted with fluoranthene reagent anions, and then analyzed via an FTICR mass analyzer. The hexapole trap allows for a broad fragment ion mass range and a high ion storage capacity. Using a 3,T FTICRMS, resolutions of 60,000 were achieved with mass accuracies averaging below 1.4,ppm. The high resolution, high mass accuracy ETD spectra provided by FTICR obviates the need for proton transfer reaction (PTR) charge state reduction of ETD product ions when analyzing proteins or large peptides. This is demonstrated with the ETD of ubiquitin and apomyoglobin yielding sequence coverages of 37 and 20%, respectively. We believe this represents the first reported successful combination of ETD and a FTICRMS. Copyright © 2008 John Wiley & Sons, Ltd. [source] Electrospray ionization mass spectrometric studies of some imidazole amidoximes and nitrolic acids and their estersRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 7 2006Larisa Oresmaa The fragmentations of the [M+H]+ ions of imidazole amidoximes, and nitrolic acids and their esters, were studied by collision-induced dissociation experiments and by determining the accurate masses of the product ions on an electrospray ionization Fourier transform ion cyclotron resonance mass spectrometer. The fragmentation pathways of the amidoximes varied with the substituent in the imidazole ring at position 1N, allowing two regioisomers to be distinguished. Nitrolic acids decompose in solution to nitrile oxides, and the studied nitrolic acid behaved in the same way in the gas phase. The esters decompose similarly to their parent compounds. Copyright © 2006 John Wiley & Sons, Ltd. [source] | ||||||||||