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Dynamics of intact immunoglobulin G explored by drift-tube ion-mobility mass spectrometry and molecular modeling

Kamila J Pacholarz1, Massimiliano Porrini, Rachel A Garlish

  • 1The EastChem School of Chemistry, University of Edinburgh, West Mains Road, EH9 3JJ, Edinburgh (UK).

Angewandte Chemie (International Ed. in English)
|June 12, 2014
PubMed

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.

Keywords:
conformation analysisimmunoglobulin Gmass spectrometrymolecular dynamicsprotein structures

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