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  • Wiley-Blackwell  (16)
  • 1990-1994  (16)
  • 1
    Electronic Resource
    Electronic Resource
    Collisionally activated dissociation and tandem mass spectrometry of intact hemoglobin β-chain variant proteins with electrospray ionization (1993)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 22 (1993), S. 112-120 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Electrospray ionization collisionally activated dissociation (CAD) mass spectra of multiply charged human hemoglobin β-chain variant proteins (146 amino acid residues, 15.9 kDa), generated in the atmospheric pressure/vacuum interface and in the collision quadrupole of a triple-quadrupole mass spectrometer, are shown and compared. Several series of structurally informative singly and multiply charged b- and y-mode product ions are observed, with cleavage of the Thr 50-Pro 51 CO—NH bond to produce the complementary y96 and b50 sequence ions as the most favored fragmentation pathway. The eight different β-globin variants studied differ by a single amino acid substitution and can be differentiated from the observed m/z shifts of the assigned product ions. The overall fragmentation patterns for the variant polypeptides are very similar, with the exception of the Willamette form, in which Arg is substituted for Pro- 51, and multiply charged y96 product ions are not observed. Circular dichroism spectra of normal βA and βWillamette show very little difference under a variety of solvent conditions, indicating that fragmentation differences in their respective CAD mass spectra are substantially governed by primary rather than secondary structure.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200220203
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The observation of non-covalent interactions in solution by electrospray ionization mass spectrometry: Promise, pitfalls and prognosis (1993)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 22 (1993), S. 493-501 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200220902
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Direct observation of a DNA quadruplex by electrospray ionization mass spectrometry (1993)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 22 (1993), S. 181-183 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In 10 mM sodium phosphate, pH 7.6, containing 0.1 mM ethylenediaminetetraacetic acid, ions corresponding to the non-covalent, four-stranded oligonucleotide, d(CGCG4GCG)4, were detected by negative ion electrospray ionization (ESI) mass spectrometry at a low nozzle-skimmer (ΔNS) bias (-150 V), but not at a higher ΔNS bias (〉 -250 V). In contrast, when the sample was desalted and analyzed by ESI mass spectrometry at a low ΔNS bias only ions for the single-stranded d(CGCG4GCG) species were observed. These data agree with spectroscopic evidence which showed that oligonucleotides with the sequence motif 5′d(CGCGnGCG)3′, where n = 2-5, formed stable four-stranded complexes in the presence of monatomic cations, like K+, Ca2+, Na+ and Li+, but not in their absence.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200220307
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  • 4
    Electronic Resource
    Electronic Resource
    Time-base modulation for the correction of cyclotron frequency shifts observed in long-lived transients from fourier-transform ion-cyclotron-resonance mass spectrometry of electrosprayed biopolymers (1993)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 7 (1993), S. 700-703 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: The occurrence of small shifts in the cyclotron frequency during the acquisition of very long transients (in excess of 80 s) has been observed to be a limiting factor for ultrahigh-resolution mass measurements of protein ions performed with electrospray-ionization Fourier-transform ion-cyclotron-resonance mass spectrometry. Resolution measurements were restricted to values less than 106 because of the frequency shifts. Measurements of the frequency shifts, performed by sequentially transforming small segments of the transient, allowed the shift to be characterized and fitted to a 4th-order equation. The sampling rate of the acquired transient was then modulated (at a rate equal to the reciprocal of the rate for the frequency shift) to allow ultrahigh resolution, greater than 2 × 106, and improved mass measurement and precision to be achieved for a small protein.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290070803
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Reduced elution speed detection for capillary electrophoresis/mass spectrometry (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Microcolumn Separations 5 (1993), S. 57-62 
    Details
    ISSN: 1040-7685
    Keywords: capillary electrophoresis ; electrospray ionization ; mass spectrometry ; reduced field strength ; peptides ; proteins ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A combined capillary electrophoresis/mass spectrometry (CE/MS) method is described that provides an increase in the efficiency of analysis by decreasing the analyte elution rate into an electrospray ionization (ESI) interface. The method is readily implemented by instituting a step change in the CE electric field strength for desired periods of time during a separation. As a result, the m/z range or the number of times an m/z range can be scanned while a solute elutes is increased by a factor proportional to the decrease in CE electric field strength. In addition, the method is shown not to cause any significant loss in separation quality as demonstrated for mixtures of proteins and peptides, while providing an effective gain in sensitivity. This allows an enhancement in the quality of mass spectra recorded while scanning wide m/z ranges. Mass spectra for a set of standard proteins were obtained for injections of 60 femtomole/protein, while analysis of an albumin tryptic digest was obtained for injections corresponding to 40 femtomoles of protein.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mcs.1220050109
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  • 6
    Electronic Resource
    Electronic Resource
    Solvent-induced conformational changes of polypeptides probed by electrospray-ionization mass spectrometry (1991)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 5 (1991), S. 101-105 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: Electrospray-ionization (ESI) mss spectrometry is used to monitor higher order structural changes of polypeptide induced by alteration of the pH or organic solvent composition in the protein solution environment. A bimodal charge-state disribution is observed in the ESI mass spectrometry of ubiquitin (relative molecualr mass 8565) in solution containing small amounts (〈20%) of organic solvents. The distribution of peaks at high m/z (low-charge state) is found to represent the protein in its native, globular state; the higher-charge-state distribution is characteristic for a more extended conformation. Addition of methanol denaturant in excess of 40% v/v is needed to eliminate the low-charge-state distribution completely. Lesser amounts of acetonitrile, acetone, or isopropanol (∼20%) are reqiored to denature the ubiquitin protein. Other proteins showing conformational efects in their ESI mass spectra are also illustrated. While the ESI spectra are related to solution phase structure, ESI-tandem mass spectrometry of multiply charged molecular ions of different conformation is suggested as a probe of gas-phase protein three-dimensional structure.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290050303
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  • 7
    Electronic Resource
    Electronic Resource
    Selected-ion accumulation from an external electrospray ionization source with a fourier-transform ion cyclotron resonance mass spectrometer (1993)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 7 (1993), S. 914-919 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: The coupling of an electrospray ionization (ESI) source to a Fourier-transform ion cyclotron resonance (FTICR) mass spectrometer provides a facility for the high resolution, accurate mass analysis of large biopolymers. Typically the m/z range of the electrosprayed ions injected and trapped in the FTICR cell is between m/z 500 and 2500 (but can vary considerably with solution conditions). Recent reports on quadrupole excitation have demonstrated the ability to cool the magnetron motion of ions trapped in the FTICR mass spectrometer cell by converting this motion to cyclotron motion which, under appropriate pressure conditions, damps readily to the center of the cell. The use of a broadband waveform (swept frequency or stored waveform inverse Fourier-transform) for the quadrupole cooling pulse was shown to provide cooling of a wide range of m/z ions, while implementation of a single frequency demonstrated a much narrower m/z response. This report demonstrates the successful combination of single-frequency quadrupole cooling with external injection of electrosprayed ions into an FTICR mass spectrometer for m/z selected-ion accumulation. This capability is particularly significant with electrospray ionization since it allows ions of only one charge state to be accumulated in the cell, and greatly increases the potential dynamic range of ESI-FTICR.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290071012
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  • 8
    Electronic Resource
    Electronic Resource
    Small volume and low flow-rate electrospray lonization mass spectrometry of aqueous samples (1993)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 7 (1993), S. 1017-1021 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: A new electrospray ionization source (emitter) has been developed which allows the effective utilization of very small sample volumes at much lower flow rates than previously demonstrated. A small diameter etcched-tip capillary has been incorporated into a pressure-infusion electrospray ionization source. The ability to electro-spray aqueous solutions without the use of an ancillary sheath flow is demonstrated with several biopolymers. High signal intensities and stable signals are observed for this source in a comparison with a standard methanol-sheath source.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290071111
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  • 9
    Electronic Resource
    Electronic Resource
    Internal energy effects in the collision-induced dissociation of large biopolymer molecular ions produced by electrospray ionization tandem mass spectrometry of cytochrome c (1990)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 4 (1990), S. 54-57 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: The effects of internal energy upon metastable and collision-induced dissociation (CID) processes observed in the tandem mass spectrometry of multiply protonated molecules of horse-heart cytochrome c (Mr 12360) are described. The internal energy of the multiply protonated (15H+) molecules (at m/z 825) formed by electrospray ionization (ESI) was manipulated using electric fields in the atmospheric pressure/vacuum interface region. Highly efficient CID is obtained for molecular ions collisionally activated in the ESI interface. The dissociation efficiency at 3.8 eV to 5.8 eV (center of mass) collision energies for internally “hot” molecular ions under multiple collision conditions in a triple quadrupole mass spectrometer is shown to be much greater than for “cold” ions. The CID spectra show dramatic effects due to internal energy, with charge stripping dominating for cold ions (where CID efficiency is very low) and extensive fragmentation observed for hot ions.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290040205
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  • 10
    Electronic Resource
    Electronic Resource
    Protein structural effects in gas phase ion/molecule reactions with diethylamine (1992)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 6 (1992), S. 159-165 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: The relationship between gas-phase protein structure and ion/molecule reactivity is explored in comparisons between native and disulfide-reduced aprotinin, lysozyme, and albumin. Reactions are performed in the reactions with equal concentrations of diethylamine, multiply protonated molecules generated by electrospray ionization (ESI) of ‘native’ proteins shifted to lower charge states than did multiply protonated molecules from ESI of the disulfide-reduced counterparts, suggesting that the disulfide-reduced protein ions are less reactive than native protein ions of the same charge state. Differences in reactivity may arise from protonation of different amino acid residues and/or differences in the proximites of charge sites in two molecules. These results suggest that the reactivity of multiply charged proteins can be significantly affected by their gas-phase structure.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290060302
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