1996
DOI: 10.1002/(sici)1096-9888(199605)31:5<555::aid-jms324>3.0.co;2-f
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Broadband Quadrupolar Axialization of Large Multiply Charged Ions to Enhance Measurement and Minimize Conformational Restrictions

Abstract: For high‐resolution Fourier transform mass spectrometry of electrosprayed proteins, the signal‐to‐noise ratio of measuring nozzle–skimmer fragment ions can be improved substantially by their broadband quadrupolar axialization (QA), even without increasing their concentration in the ion cyclotron resonance cell. Axialization of the product ions makes possible larger, more concentric ion orbits for measurements. QA allowed the identification of new sequence‐indicative product ions from a 29 kDa protein. However,… Show more

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Cited by 15 publications
(23 citation statements)
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“…Conformations and folding of proteins in the gas phase have recently been reported by McLafferty and co-workers (Suckau et al, 1993;O'Connor et al, 1996). These studies have used electrospray ionization coupled with FTMS to study the protein folding of cytochrome c by monitoring 'H/D exchange in the gas phase.…”
Section: 'H/d Exchangementioning
confidence: 91%
“…Conformations and folding of proteins in the gas phase have recently been reported by McLafferty and co-workers (Suckau et al, 1993;O'Connor et al, 1996). These studies have used electrospray ionization coupled with FTMS to study the protein folding of cytochrome c by monitoring 'H/D exchange in the gas phase.…”
Section: 'H/d Exchangementioning
confidence: 91%
“…For example, substituting acetonitrile for water can severely reduce enzymatic activity, even though the α-helix content and crystalline enzyme structure are little changed . Even with the complete removal of water and its concomitant hydrophobic stabilization, gaseous protein cations can exist in several conformational states that can be folded and unfolded. , In a critical mechanistic examination of such data for cytochrome c ,10b Wolynes pointed out 2 that van der Waals packing forces would have to be unusually important for native structures to survive in vacuo, without solvent stabilization, so that many other structures should be competitive energetically. Although the absence of water should increase the stability of classical secondary structures such as the α-helix and β-sheet, the apolar vacuum could even stabilize hydrophobic residues on the exterior to produce an “inside out” conformation .…”
Section: Introductionmentioning
confidence: 99%
“…After its introduction at ISOLTRAP [1] as a preparatory step for precision mass spectrometry of short-lived radionuclei [2,3], the method has quickly been transferred [4] to (Fourier transform) ion cyclotron resonance (FT-ICR) cells. In analytical chemistry applications it is often implemented as part of the standard procedure of complex event sequences, either for axialization of particular species [5] or broader ranges of mass-over-charge ratios [6].…”
Section: Introductionmentioning
confidence: 99%