title: Dynamics of intact immunoglobulin G explored by drift-tube ion-mobility mass spectrometry and molecular modeling.
abstract: Collision cross-sections (CCS) of immunoglobulins G1 and G4 have been determined using linear drift-tube ion-mobility mass spectrometry. Intact antibodies and Fc-hinge fragments present with a larger range of CCS than proteins of comparable size. This is rationalized with MD simulations, which indicate significant in vacuo dynamics between linked folded domains. The IgG4 subclass presents over a wider CCS range than the IgG1 subclass.
authors.affiliation: The EastChem School of Chemistry, University of Edinburgh, West Mains Road, EH9 3JJ, Edinburgh (UK).
authors.forename: Kamila J
authors.initials: KJ
authors.lastname: Pacholarz
authors.forename: Massimiliano
authors.initials: M
authors.lastname: Porrini
authors.forename: Rachel A
authors.initials: RA
authors.lastname: Garlish
authors.forename: Rebecca J
authors.initials: RJ
authors.lastname: Burnley
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Taylor
authors.forename: Alistair J
authors.initials: AJ
authors.lastname: Henry
authors.forename: Perdita E
authors.initials: PE
authors.lastname: Barran
mesh_terms: D007074:Immunoglobulin G / Q000737:chemistry*; D013058:Mass Spectrometry / Q000379:methods*; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D007074:Immunoglobulin G
keywords: conformation analysis; immunoglobulin G; mass spectrometry; molecular dynamics; protein structures