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The sample was received as a solid sample and was dissolved into water with 0.1% formic acid and serially diluted to final test concentrations with the same water/0.1% formic acid solvent.   For samples analyzed by liquid chromatography, an Evosep One UHPLC (Evosep, Odense, Denmark) was used.  Samples were prepared onto the Evotips using the standard Evosep method.  All analyses with Evosep used the standard, preconfigured Evosep methods with no modifications.  Mobile phases A and B were water with 0.1% formic acid (v/v) and 100% acetonitrile with 0.1% formic acid (v/v), respectively.  For 200 SPD methods, samples were separated on a 4 cm x 150 µm i.d reversed-phase column packed with 1.5 µm C18-coated porous silica beads (EV1109). The outlet of the LC columns (with the exception of the Ion Optiks column) was connected to an Evosep EV1116 Agilent Sleeve Adapter fitted with a 30 µm stainless steel nanospray emitter (Evosep EV1086) mounted in a custom holder and positioned in front of the capillary inlet of the HRIM/quadrupole-time-of-flight mass spectrometer (HRIM/Q-TOF MS).  A prototype high-resolution ion mobility spectrometer/quadrupole time-of-flight mass spectrometer was used for analysis (HRIM/Q-TOF).   The HRIM spectrometer is based on a MOBILion MOBIE® system (MOBILion Systems, Chadds Ford, PA) and was coupled with one of two different Agilent Q-TOF mass spectrometers (6546 or 6545, Agilent, Santa Clara, CA).  Ions produced in by nanoelectrospray ionization in the inlet region of the mass spectrometer entered the vacuum region of the instrument through a glass capillary and passed through a dual-narrow ion funnel to collect and focus ions on the inlet of the HRIM module.  Ions that enter the ion mobility region are confined between the two printed-circuit board (PCB) electrodes by RF voltage fields.  A traveling voltage wave moves ions along a serpentine path on the PCB electrodes to a region where ions are accumulated for some period prior to ion mobility separation.  Ions are released onto the long serpentine separation path while the next set of ions is accumulated in parallel.  Ions are moved through the separation path with a traveling wave voltage that varies in both frequency and amplitude to improve resolving power24. After mobility separation, ions are guided into the Q-TOF for either precursor mass analysis or collision-induced dissociation (CID) followed by fragment mass analysis, producing alternating ion mobility frames of low collision energy with precursor ions only and ion mobility frames with high collision energy with fragment ions corresponding to the precursor ions from the previous frame.  For experiments where no ion mobility separation is desired, the ion mobility portion of the instrument can be configured to allow all ions to pass through for standard Q-TOF mass analysis without any prior mobility separation. Passthrough operation was used to collect data-dependent acquisition (DDA) data used as an instrumental baseline.  After mass analysis, detected ion current was digitized and converted into mass spectral data which was saved as result files with relevant information including retention time, arrival time for ion mobility separation, mass-to-charge, and intensity for all data points."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["After collecting data, processing was done using third party software to identify and quantify the protein groups and peptides found within the analyzed samples. For ion mobility data, the data were processed with a library free search using Spectronaut v19 (Biognosys, Schlieren, Switzerland). DDA data were processed and reviewed using Skyline Targeted Mass Spectrometry Environment."],"omics_type":["Proteomics"],"labhead":["Daniel DeBord"],"instrument_platform":[""],"labhead_affiliation":["MOBILion Systems, Inc., US"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["leonard.rorrer@mobilionsystems.com"],"publication":["42331252 Rorrer LC, Deng L, Royer L, Uribe I, Orsburn BC, Bernhardt O, Gandhi T, Reiter L, DeBord D. A Parallel Accumulation-Mobility Aligned Fragmentation Strategy Utilizing High-Resolution Ion Mobility for High Performance Proteomics Analysis. Mol Cell Proteomics. 2026:101608 10.1016/j.mcpro.2026.101608"],"submitter_affiliation":["MOBILion Systems, Inc."],"submitter_country":["United States"],"pubmed_abstract":["Here we present a novel data independent acquisition (DIA) mass spectrometry (MS) operating mode termed parallel accumulation-mobility aligned fragmentation (PAMAF) that offers enhanced speed and sensitivity of ion fragmentation analysis for discovery workflows such as bottom-up proteomics. This mode of operation leverages high-resolution ion mobility (HRIM) separation capabilities of the structures for lossless ion manipulation (SLIM) technology to achieve HRIM-based precursor isolation in place of traditional quadrupole filtering approaches. PAMAF mode increases the number of features that can be identified per MS1/MS2 acquisition cycle by employing mobility-based time alignment to associate fragment ions with their corresponding precursor ions. By using a high-speed, lossless separation technique for precursor isolation instead of the comparatively slow and wasteful quadrupole filtering, ion losses are avoided while simultaneously increasing the rate at which precursor ions are sequentially fragmented and detected. Additionally, by accumulating ions while the previous packet of ions is being analyzed, the PAMAF mode achieves ∼100% ion utilization efficiency. Benchmarking results of LC-PAMAF-MS analysis of a whole cell protein digest showed ∼6x more protein group identifications compared to a standard data-dependent acquisition (DDA) analysis without HRIM on the same QTOF instrument, and to >100x improvement for low-load workflows. Quantitative evaluations demonstrated that PAMAF mode could quantify low abundance peptides, including those undetectable by DDA. Additionally, since precursor isolation in PAMAF mode is size-based rather than m/z-based, coeluting isobars and isomers can be resolved prior to fragmentation, eliminating chimeric spectra that compromise identification accuracy. We also explored the benefits of combining HRIM and quadrupole isolation to achieve improved specificity termed DIA-PAMAF mode, which enabled the detection of over 8,000 protein groups from a HeLa digest analysis. PAMAF mode brings a powerful new technique to the field of proteomics with the potential to improve the sensitivity and selectivity of mass spectrometry-based proteomics."],"pubmed_title":["A Parallel Accumulation-Mobility Aligned Fragmentation Strategy Utilizing High-Resolution Ion Mobility for High Performance Proteomics Analysis."],"pubmed_authors":["Rorrer Leonard C LC, Deng Liulin L, Royer Lauren L, Uribe Isabel I, Orsburn Benjamin C BC, Bernhardt Oliver O, Gandhi Tejas T, Reiter Lukas L, DeBord Daniel D"],"additional_accession":[]},"is_claimable":false,"name":"A Parallel Accumulation-Mobility Aligned Fragmentation Strategy Utilizing High-Resolution Ion Mobility for High Performance Proteomics Analysis: Qual-Quan Data Sets for PAMAF and DDA Modes","description":"Here we present a parallel accumulation-mobility aligned fragmentation (PAMAF) mode that expands the capabilities of the MOBILion® Systems MOBIE® high-resolution ion mobility (HRIM) system for mass spectrometry-based proteomics.  The MOBIE system leverages structures for lossless ion manipulation (SLIM) to achieve HRIM separations within a compact footprint.  Along with the HRIM separations, which increase the number of features identified per cycle, PAMAF enables alignment of fragment ions with their precursors ions without quadrupole isolation prior to fragmentation, avoiding the ion losses up to 99%.  With PAMAF mode, ions can be accumulated in parallel to the ion mobility (IM) separation, achieving close to 100% ion utilization efficiency. Quantitative evaluations demonstrated that PAMAF mode was capable of quantifying low abundance peptides, including those undetectable by 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