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Datasets in the publication Comparison of Partially Denatured Cytochrome c Structural Ensembles in Solution and Gas Phases Using Cross-Linking Mass Spectrometry
ORGANISM(S): Equus Caballus 
Cleavable crosslinking has traditionally been employed in bottom-up mass spectrometry to elucidate protein structure and protein-protein interactions through identification of peptides bearing characteristic mass adducts. Here, we demonstrate the application of cleavable crosslinking in top-down mas...
ORGANISM(S): Homo Sapiens (human) Equus Caballus 
Raw data from the manuscript "Strategies for Acid and Amine Cross-linking and Labeling for Protein Structural Characterization Using Mass Spectrometry" in Analytical Chemistry 2025 vol 97 issue 15
ORGANISM(S): Homo Sapiens (human) 
The benefits of native mass spectrometry have led to the extensive study of proteins inside mass spectrometers in the gas phase. The expansion of native mass spectrometry requires novel tools for gaining greater insights into protein structures. Herein, we introduce a new approach utilizing gas phas...
ORGANISM(S): Homo Sapiens (human) Equus Caballus 
Recombinant human alpha synuclein crosslinked with 2.5 molar excess BS2G and BS3 crosslinkers. Buffer exchanged into 50 mM ammonium acetate. MS/MS on singly crosslinked protein by top-down ECD. Final protein concentration 50 uM. Positive mode static nanospray.
ORGANISM(S): Homo Sapiens (human) 
Agilent Tunemix samples analyzed on three IMS-MS platforms with nitrogen gas: 1) stepped-field drift tube IMS-MS, 2) single-field drift tube IMS-MS, and 3) SLIM-based IMS-MS. Also, tetraalkylammonium (TAA) salt samples analyzed with SLIM-based IMS-MS using helium gas.
ORGANISM(S): Unclassified Sequences (ncbitaxon:12908) 
2020-08-19 | MSV000085979 | MassIVE
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