Development of Ion Mobility-Mass Spectrometry as a High-throughput Approach for Structural Genomics [electronic resource].
Year: 2014
Type: article
Abstract: interactions are observed. A key challenge for protein ion mobility measurements of intact proteins is accessing local, domain-level structure information. In a third set of experiments, gas-phase protein unfolding data were acquired for a range of monomeric proteins. The unfolding of multi-domain proteins, using either collision-induced unfolding or Coulomb-associated stretching, revealed a strong, positive correlation with known protein domain structures in solution. In a final set of experiments, the protocols developed here using model protein systems are applied to two multiprotein complexes of currently unknown structure: the heme oxygenase-2/cytochrome P450 reductase dimer and the human mitochondrial ribonuclease P hetero-hexamer. In these cases, IM-MS aided by elucidating either the chemical nature of the protein contacts or coarse-grained topologies of the complexes studied.
Author: Zhong, Yueyang.
Language: English
Subfield: Spectroscopy
Field: Chemistry
Domain: Physical Sciences
Open Access status: green
OpenAlex ID: W7055852419