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ProteomicsSelf-packed size-exclusion columns enable versatile high-throughput native, top-down, and ion-mobility-mass spectrometry studies on proteins and complexes.
Native MS (nMS) is a key structural biology technique that makes it possible to study intact proteins and their interactions. Unfortunately, non-volatile salts are incompatiblewith nMS, which demands a laborious desalting procedure. Non-denaturing size exclusion chromatography (SEC) allows both rapi...
ORGANISM(S): Bos taurus (Bovine) Candida albicans (Yeast) Homo sapiens (Human) Escherichia coli Gallus gallus (Chicken) Equus caballus (Horse) 
2025-06-29 | PXD061452 | Pride
Ligand screening Top-down proteomics Native mass spectrometry Size-exclusion chromatography Protac Ion mobility 
ProteomicsLeveraging Parameter Dependencies in High-Field Asymmetric Waveform Ion-Mobility Spectrometry and Size-exclusion Chromatography for Proteome-wide Crosslinking Mass Spectrometry_protein ID dataset
Ion mobility spectrometry shows great promise to tackle analytically challenging research questions by adding another separation dimension to liquid chromatography-mass spectrometry. The understanding of how analyte properties influence ion mobility has increased through recent studies but no clear ...
ORGANISM(S): Homo Sapiens (human) 
2022-12-16 | PXD022341 | JPOST Repository
ProteomicsAutomating Multidimensional Liquid Chromatography, Ion Mobility Spectrometry and Mass Spectrometry Data Analyses Using Skyline
Recent advances in ion mobility spectrometry (IMS) have illustrated its power in the structural characteristics of a molecule, especially when coupled with other separations dimensions such as liquid chromatography (LC) and mass spectrometry (MS). However, these three separation techniques together ...
ORGANISM(S): Bos Taurus Saccharomyces Cerevisiae 
PXD010650 | panorama
UnknownSizing up DNA nanostructure assembly with native mass spectrometry and ion mobility.
Not available
S-EPMC9232653 | biostudies-literature
UnknownProtein shape sampled by ion mobility mass spectrometry consistently improves protein structure prediction.
Not available
S-EPMC9334640 | biostudies-literature
ProteomicsOrbitrap mass spectrometry and high-field asymmetric waveform ion mobility spectrometry (FAIMS) enable the indepth analysis of human serum proteoforms
In this study, we describe a straightforward protocol for intact proteoform sample preparation based on depletion of albumin and immunoglobulins followed by simplified fractionation of remaining serum proteins via polyacrylamide gel electrophoresis. After molecular weight-based fractionation, we sup...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-08-02 | MSV000092574 | MassIVE
UnknownCharacterization of Molecular Tweezer Binding on α-Synuclein with Native Top-Down Mass Spectrometry and Ion Mobility-Mass Spectrometry Reveals a Mechanism for Aggregation Inhibition.
Not available
S-EPMC10959575 | biostudies-literature
UnknownEvaluation of Surface-Induced Dissociation Ion Mobility-Mass Spectrometry for Lipid Structural Characterization.
Not available
S-EPMC11798589 | biostudies-literature
ProteomicsOrbitrap mass spectrometry and high-field asymmetric waveform ion mobility spectrometry (FAIMS) enable the in-depth analysis of human serum proteoforms
After molecular weight-based fractionation, we supplemented the traditional liquid chromatography tandem mass spectrometry (LC-MS2) data acquisition with high-field asymmetric waveform ion mobility spectrometry (FAIMS), which served as an additional separation dimension to further simplify serum pro...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-02-16 | MSV000091309 | MassIVE
UnknownNative mass spectrometry and ion mobility characterization of trastuzumab emtansine, a lysine-linked antibody drug conjugate.
Not available
S-EPMC4534172 | biostudies-literature
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