title: Collisional and Coulombic unfolding of gas-phase proteins: high correlation to their domain structures in solution.
abstract: The three-dimensional structures adopted by proteins are predicated by their many biological functions. Mass spectrometry has played a rapidly expanding role in protein structure discovery, enabling the generation of models for both proteins and their higher-order assemblies. While important coursed-grained insights have been generated, relatively few examples exist where mass spectrometry has been successfully applied to the characterization of protein tertiary structure. Here, we demonstrate that gas-phase unfolding can be used to determine the number of autonomously folded domains within monomeric proteins. Our ion mobility-mass spectrometry data highlight a strong, positive correlation between the number of protein unfolding transitions observed in the gas phase and the number of known domains within a group of sixteen proteins ranging from 8-78 kDa. This correlation and its potential uses for structural biology is discussed.
authors.affiliation: Department of Chemistry, University of Michigan, 930 North University Avenue, Ann Arbor, MI 48109-1055 (USA).
authors.forename: Yueyang
authors.initials: Y
authors.lastname: Zhong
authors.forename: Linjie
authors.initials: L
authors.lastname: Han
authors.forename: Brandon T
authors.initials: BT
authors.lastname: Ruotolo
mesh_terms: D005740:Gases / Q000737:chemistry*; D013058:Mass Spectrometry; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry*; D012996:Solutions
chemical_list: D005740:Gases; D011506:Proteins; D012996:Solutions
keywords: gas-phase structures; mass spectrometry; protein folding; protein structures