Publications by authors named "Shoushuai Fu"
Article Synopsis
- A new racetrack field asymmetric waveform ion mobility spectrometry (r-FAIMS) device combines cylindrical and planar sections to enhance the sensitivity and resolution for analyzing peptide structures.
- The r-FAIMS achieves up to 8.5 times higher ion intensity and 1.70 times better peak resolution for doubly charged bradykinin ions compared to the earlier p-FAIMS model.
- With a narrower gap width and optimal operating conditions, r-FAIMS can reach a resolving power exceeding 120 for triply charged ions, showcasing its potential for detailed biomolecular characterization.
A new racetrack field-asymmetric waveform ion mobility spectrometry (r-FAIMS) analyzer was developed in this study by combining the existing planar FAIMS (p-FAIMS) and cylindrical FAIMS (c-FAIMS). The ion inlet and outlet regions of r-FAIMS were consisted of a half of c-FAIMS, respectively, and these c-FAIMS were further connected by two p-FAIMS to form a racetrack shaped FAIMS. With such FAIMS working electrode configuration, the ions entering the r-FAIMS can be focused and separated in the first c-FAIMS section, be further separated in the p-FAIMS section with high-resolution, be focused and separated again in the final c-FAIMS section and eventually enter the mass spectrometer or other analyzers for analysis.
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