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A Tilted Surface and Ion Carpet Array for SID.

Alyssa Q Stiving, Joshua D Gilbert, Benjamin J Jones

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    This study introduces a new surface-induced dissociation (SID) device for mass spectrometry (MS). The novel design, featuring a tilted surface, effectively fragments large protein complexes and peptides while reducing device complexity.

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    Area of Science:

    • Analytical Chemistry
    • Biochemistry
    • Structural Biology

    Background:

    • Native mass spectrometry (MS) is crucial for analyzing large macromolecular systems.
    • Surface-induced dissociation (SID) is a key technique in tandem MS for protein complex structural analysis.

    Purpose of the Study:

    • To present a novel SID device design for improved analysis of peptides and protein complexes.
    • To evaluate the performance of a tilted surface and ion carpet array in a new SID device.

    Main Methods:

    • Development of a new SID device incorporating a tilted surface and ion carpet array.
    • Fragmentation of ions across a range of mass-to-charge ratios (m/z), including peptides and protein complexes.
    • Analysis of product ion collection and signal intensity at varying SID energies.

    Main Results:

    • The new SID device effectively fragments both low (peptides) and high (protein complexes) m/z ions.
    • The tilted surface design successfully reduces device dimensions and the number of tunable voltages.
    • The ion carpet array, while simplifying the device, showed limitations in product collection at higher energies for protein complexes.

    Conclusions:

    • The tilted surface in the new SID device design offers significant advantages for shortening instrumentation and reducing complexity.
    • Further optimization of the ion carpet array may be needed to enhance product collection efficiency for large protein complexes in SID-MS.