Fourier transform ion cyclotron resonance MS

Laser desorption (LD) Fourier transform ion cyclotron resonance MS (FTICR-MS) in the positive mode was applied for the analysis of... 

Hofstadler, S.A. Griffey, R.H. Pasa-Tolic, R. Smith, R.D. The Use of a Stable Internal Mass Standard for Accurate Mass Measurements of Oligonucleotide Fragment Ions Using ESI Fourier Transform Ion Cyclotron Resonance-MS With Infrared Multiphoton Dissociation. Rapid Commun. Mass Spectrom. 1998,12, 1400-1404. 

For proteomic technologies to be of widespread use, the reproducibility of each method must be determined. Several studies have been conducted to investigate the coefficient of variance associated with different technologies. One group examined a fully automated HPLC 9.4-tesla Fourier transform ion cyclotron resonance MS designed for unattended proteomics research 24 hours per day to investigate the instruments overall performance. 

Hubner, G., Lindner, B. Separation of R-form lipopolysaccharide and lipid A by CE-Fourier-transform ion cyclotron resonance MS. Electrophoresis 30 (2009) 1808-1816. 

A dual-iidet ESI source, the LockSpray , was introduced by Waters, based on the rotating aperture of the MUX-source, for the co-introduction of a reference compoimd to act as a lock-mass for accurate-mass determination [65-66]. Dual-inlet devices to introduce a lock-mass compound have also been reported for sector [67] and Fourier-transform ion-cyclotron resonance MS (FT-ICR-MS) instruments [68]. 

Due to its high resolving power and its abilities to accurate-mass determination, Fourier-transform ion-cyclotron resonance MS (FT-ICR-MS) has become an important tool in proteomics (Ch. 18.3.4-5). Its potential in phosphoprotein... 

Direct-infusion MS is a very interesting approach, especially when sample characteristics allow MS analysis with minimum sample treatment. Thus, ESI can be used to directly ionize analytes in liquid samples in a high electric field. A small flow of the liquid sample is conducted through a capillary to the high electric field for ESI. Usually, sample solutions must be carefully cleaned and filtered to avoid potential capillary blocking. Following this idea, direct-infusion ESI-FTICR (Fourier transform ion cyclotron resonance) MS of a coffee drink combined with partial least-squares multivariate statistical analysis was successfully employed to predict the blend composition of commercial coffee varieties (28). In a different work, minimal sample manipulation was carried out to obtain detailed molecular composition of edible oils and fats analyzed by flow-injection ESI-Orbitrap MS for quality assessment and authenticity control purposes (29). Commonly, when using direct infusion approaches, sample needs to be treated to dissolve the compounds of interest in the appropriate solvent. 

Attempts have been made to observe and experimentally determine the structure of Cd Is in the gas phase and study it in the condensed state. However, an unambiguous structure determination was unsuccessful. Retardation of the degenerate rearrangement was achieved by trapping the ion in clusters with H2, Cd I4, Ar, or N2. The methods include, for example, infrared (IR) spectroscopy, pulsed electron-beam MS, and Fourier transform ion cyclotron resonance MS (FT-ICR MS). ... 

The relative affinity series 24 was found for bare Au+ ions binding with various molecules M, to yield complex ions [AuM]+. This took place in the low-pressure regime of a Fourier transform ion cyclotron resonance MS. The absolute bond dissociation energies were evaluated by means of ab initio MO calculations at the MP2 level of theory255. 

Figure 9.2 The basic components of a mass spectrometer. All mass spectrometers consist of an ion source linked to a mass analyser then to a detector. The important ion sources and mass analysers for biological mass spectrometry are listed. There are many other potential ion sources and mass analysers used generally in mass spectrometry, but only the indicated are of use in the analysis of biological macromolecules and amphiphilic lipids, and also in proteomics FAB fast atom bombardment MALDI matrix-assisted laser desorption and ionization ESI electrospray ionization ToF time of flight FTICR fourier transform ion cyclotron resonance MS/MS tandem mass spectrometry.

Ion-trap methods include Fourier transform ion cyclotron resonance MS (FTICR-MS) and quadrupole ion traps (QIT or Paul traps). In these methods, ions are produced in or transferred into a region with appropriate geometry walls and some combination of magnetic fields, DC potentials, and RF potentials that confine the ions on the timescale of seconds to days. FTICR-MS has been particularly popular for the study of organometallic ions in the gas phase. In FTICR-MS, the ions are confined by a magnetic field that constrains the ions to the center of the cell. 

Pan, J., Borchers, C.H. (2013) Top-down structural analysis of posttranslationally modified proteins by Fourier transform ion cyclotron resonance-MS with hydrogen/deuterium exchange and electron capture dissociation. Proteomics, 13 (6), 974-981. 

The development of ionization techniques and mass analyzers has enabled mass spectrometrists to determine the accurate mass of small molecules as well as biomolecules that are present at low levels. The modem quadrupole time of flight (Q-TOF), Fourier transform ion cyclotron resonance MS (FT-ICR MS), and Orbitrap instruments allow determination of the mass of an ion with accuracies and precisions beyond the decimal point. Mass accuracy measurement, typically measured and reported as parts per million (ppm), is essential for elemental composition assignment. 

After the first demonstration of multiply charged gas-phase proteins ions, all major instrument manufacturers developed atmospheric-pressure ion sources, equipped with electrospray interfaces for both protein characterization and LC-MS applications. Within 5 years, electrospray interfacing became the method of choice in LC-MS coupling. It led to a large increase in the use of MS for the characterization and identification of labile and polar analytes as well as to routine quantitative analysis. The advent of electrospray ionization for peptide and protein analysis stimulated further development and analytical application of existing and new mass analysis approaches, such as quadrupole ion traps, Fourier-transform ion-cyclotron resonance MS, and quadru-pole-time-of-flight hybrid instruments. It opened new application areas, such proteomics. LC-MS... 

Other mass analyzers, especially those providing high-resolution, such as time-of-flight (ToF), Orbitrap and Fourier-transform ion cyclotron resonance MS, have been applied scarcely. Two biotransformation studies were carried out with a QqTOF-MS/MS, these advantages were used in order to gather accurate masses of metabolites [17, 60] and recently, the ultra-high resolution Orbitrap MS has been applied to confirm the presence of novel metabolites [21],... 

Laser desorption/Fourier transform ion cyclotron resonance MS has also been used to identify and determine the following types of polymer additives [74] UV absorbents, e.g., Tinuvin [75], antioxidants, e.g., Irganox MD-1024, and amide wax antislip additives. 

More recently, the use of liquid chromatography and tandem MS (LC/MS/MS) has also eased purification and recovery methods. For instance, Vamum and colleagues utilized gel-free two-dimensional capillary LC/MS/MS and Fourier transform ion cyclotron resonance MS to identily and determine the relative abundances of viral and cellular proteins in purified HCMV virions and dense bodies. Analysis of the proteins Irom purified HCMV virion preparations has indicated that the particle contains significantly more viral proteins than previously known. They identified more than 71 HCMV-encoded proteins and 70 host cellular proteins in HCMV virions, which included cellular structural proteins, enzymes, and chaperones [6]. Another study using LC/MS/MS for the adenovirus type 5 pro-teome found a total of 11 protein species from 154 peptides, at a sensitivity of 10 copies per virus and a detection limit of 70 finol for two proteins [36]. 

Following gradient purification of virions, LC/MS/MS was used to identify the components of the HCMV virion [6]. The results were verified by coupling high-accuracy mass measurements with LC and FT-ICR (Fourier transform ion cyclotron resonance) MS. Fifty-nine proteins were identified including 12 proteins encoded by known HCMV ORFs not previously known to reside in virions. The classes of proteins identified included capsid proteins, tegument proteins, glycoproteins, and 12 proteins involved in DNA replication and transcription. Additionally, 12 more viral polypeptides were identified that had not been previously characterized [6]. 

Liang, Z., A. G. Marshall, D. G. Westmoreland, Molecular weight distributions of rtrr-OPE by laser desorption Fourier transform ion cyclotron resonance MS and HPLC, Anal. Chem., 1991,65,815-818. 

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