Isotopic Resolution of Protein Complexes up to 466 kDa Using Individual Ion Mass Spectrometry
Year: 2020
Type: article
Abstract: High Resolution Image Download MS PowerPoint Slide Native mass spectrometry involves transferring large biomolecular complexes into the gas phase, enabling the characterization of their composition and stoichiometry. However, the overlap in distributions created by residual solvation, ionic adducts, and post-translational modifications creates a high degree of complexity that typically goes unresolved at masses above ∼150 kDa. Therefore, native mass spectrometry would greatly benefit from higher resolution approaches for intact proteins and their complexes. By recording mass spectra of individual ions via charge detection mass spectrometry, we report isotopic resolution for pyruvate kinase (232 kDa) and β-galactosidase (466 kDa), extending the limits of isotopic resolution for high mass and high m / z by >2.5-fold and >1.6-fold, respectively.
Source: Analytical Chemistry
Language: English
Subfield: Spectroscopy
Field: Chemistry
Domain: Physical Sciences
Open Access status: bronze
Awards: Defining native proteoform landscape for amyloid-beta in Alzheimers disease, Alzheimer's Disease Characterization via a Novel Native Mass Spectrometry Platform, G2124791380, National Resource for Translational and Developmental Proteomics, Acquisition of a Thermo Fisher Scientific Q Exactive UHMR mass spectrometer, Neurometabolomics and Neuroproteomics Center on Cell-Cell Signaling
OpenAlex ID: W3110774789