{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD078350/meta-data_HYE.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD078350/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD078350/1000ng_HYE_MIX-B_htrms_files.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD078350/1000ng_HYE_MIX-A_mbi_files.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD078350/20260209_102620_1000ng_HYE_XIM_0.5_htrms_directDIA_Report_HYE_in_MSstats.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD078350/1000ng_HYE_MIX-B_mbi_files.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD078350/1000ng_HYE_MIX-A_htrms_files.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["daniel.debord@mobilionsystems.com"],"submitter":["Leonard Rorrer"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Hela","Yeast","Pamaf","Ion mobility","Hye","Slim","Hrim","Qtof","Bottom-up proteomics","E. coli"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD078350"],"tissue":["Cell Suspension Culture","Cell Culture"],"sample_protocol":["The Human/Yeast/Escherichia coli (HYE) tri-species mixtures (P/Ns E5H65Y30 and E20H65Y15, ProTec Diagnostics GmbH, Greifswald, Germany) combine human (H), yeast (Y), and E.coli (E) proteomes in two formulations: Mix A containing 65% H, 30% Y, and 5% E, and Mix B containing 65% H, 15% Y, and 20% E.  These samples were received as lypholized powders of trypsin digested proteins and were reconstituted in water with 0.1% formic acid and serially diluted to final concentration. Additionally, to aid in retention time calibration for the HYE samples analyzed by liquid chromatography, Indexed Retention Time calibration peptides were added (Biognosys iRT Kit, P/N 1816351, Bruker, Billerica, MA).  An Evosep One UHPLC (Evosep, Odense, Denmark) was used for liquid chromatography. Samples were prepared on 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 30 samples per day (SPD) methods, samples were separated on a 15 cm x 150 µm i.d. reversed-phase column packed with 1.5 µm C18-coated porous silica beads heated to 40°C (Evosep EV 1137). The outlet of the LC columns 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 HRIM/Q-TOF MS was used for analysis. The HRIM spectrometer is based on a MOBIE® system (MOBILion Systems, Chadds Ford, PA) and was coupled to one of two Agilent Q-TOF mass spectrometers (6546 or 6545, Agilent, Santa Clara, CA). Ions produced 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 (DNIF) to collect and focus ions into the inlet of the HRIM module. Ions that enter the ion mobility region are confined between printed-circuit boards (PCBs) by RF electrical fields. A phase-shifted AC waveform (i.e. traveling wave) applied to a repeating sequence of PCB electrodes moves ions to an on-board accumulation (OBA) region where they are accumulated for some period prior to ion mobility separation. Ions are released into 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 during the mobility separation to improve resolving power across the mobility range. 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 (precursor ion detection) and ion mobility frames with high collision energy, detecting fragment ions corresponding to the precursor ions from the previous frame.  For the high collision energy (MS2) ion mobility frame, the collision energy was ramped to provide optimal collision energy per m/z values of peptides according to their anticipated mobility arrival times. 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":["Four replicates of each mixture were acquired in PAMAF mode. The data were processed in Spectronaut v20 (Biognosys, Schlieren, Switzerland) using the directDIA+ workflow with a combined three-proteome search across all MIX-A and B replicates. Default settings were used except for the following: the precursor q-value cutoff, precursor PEP cutoff, protein q-value cutoff (experiment), protein q-value cutoff (run), and protein PEP cutoff were all set to 0.01 and the XIC IM extraction window correction factor was set to 0.5. The Spectronaut report was exported using the MSStats Report (v 3.7.3) format with the addition of the “PG.Organisms” and “FG.MS1RawQuantity” columns for downstream analysis. The fragment-level Spectronaut report was collapsed to the precursor-level and the “FG.MS1RawQuantity” was substituted for the “F.PeakArea” values which were read into  MSstats for preprocessing,   followed by protein-level summary without data normalization or imputation. Using a custom R workflow, protein group IDs were filtered to include only those with measurements in all four replicates of each mix and then the normalization factors for only human proteins were calculated and applied to the yeast and E. Coli data. Scatter, box, and distribution plots were generated in R using ggplot2."],"omics_type":["Proteomics"],"labhead":["Daniel DeBord"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["MOBILion Systems, Inc"],"species":["Homo Sapiens (human)","Escherichia Coli","Saccharomyces Cerevisiae (baker's Yeast)"],"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 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. In addition, 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 ∼6× more protein group identifications compared to a standard data-dependent acquisition analysis without HRIM on the same QTOF instrument, and >100 x improvement for low-load workflows. Quantitative evaluations demonstrated that PAMAF mode could quantify low abundance peptides, including those undetectable by data-dependent acquisition. In addition, 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 8000 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: HYE Quantification Data Sets for PAMAF Mode","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 precursor 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. Here, we demonstrate deep proteome coverage and robust LFQ accuracy and precision using PAMAF on a HRIM-QTOF 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