Electron-capture dissociation and ion mobility mass spectrometry for characterization of the hemoglobin protein assembly.

摘要: Native spray has the potential to probe biophysical properties of protein assemblies. Here we report an investigation using both ECD top-down sequencing with FTICR mass spectrometer and ion mobility (IM) measurements on a Q-TOF investigate collisionally induced unfolding native-like heterogeneous tetrameric assembly, human hemoglobin (hHb), in gas phase. To our knowledge, this is first combining ion-mobility data same target assembly delineate effects collisional activation size extent location fragmentation. Although collision-induced clearly seen by IMMS ECD, latter delineates regions that increasingly unfold as collision energy increased. The results are consistent previous outcomes for homogeneous assemblies reinforce interpretation opens structure from flexible make available fragmentation, without dissociating component proteins.