biostudies-literatureUnknown11(1)Azegami NThe contribution of disordered regions to protein function and structure is a relatively new field of study and of particular significance as their function has been implicated in some human diseases. Our objective was to analyze various deletion mutants of the bromodomain-containing protein 4 (BRD4) using native mass spectrometry to characterize the gas-phase behavior of the disordered region connected to the folded domain. A protein with a single bromodomain but no long disordered linker displayed a narrow charge distribution at low charge states, suggesting a compact structure. In contrast, proteins containing one or two bromodomains connected to a long disordered region exhibited multimodal charge distributions, suggesting the presence of compact and elongated conformers. In the presenMass spectrometry (Tokyo, Japan)A0110https://www.ebi.ac.uk/biostudies/studies/S-EPMC9853951biostudies-literatureNative Mass Spectrometry of BRD4 Bromodomains Linked to a Long Disordered Region.PMC9853951Azegami NAkashi SSuzuki NKonuma TTaguchi RSakata YfalseNative Mass Spectrometry of BRD4 Bromodomains Linked to a Long Disordered Region.The contribution of disordered regions to protein function and structure is a relatively new field of study and of particular significance as their function has been implicated in some human diseases. Our objective was to analyze various deletion mutants of the bromodomain-containing protein 4 (BRD4) using native mass spectrometry to characterize the gas-phase behavior of the disordered region connected to the folded domain. A protein with a single bromodomain but no long disordered linker displayed a narrow charge distribution at low charge states, suggesting a compact structure. In contrast, proteins containing one or two bromodomains connected to a long disordered region exhibited multimodal charge distributions, suggesting the presence of compact and elongated conformers. In the presen2022-01-01T00:00:00Z20222026-07-15T22:26:26.052Z2025-04-06T18:03:16.989ZS-EPMC98539513671380810.5702/massspectrometry.A0110