Hydrogen exchange mass spectrometry reveals protein interfaces and distant dynamic coupling effects during the reversible self-association of an IgG1 monoclonal antibody

Jayant AroraDepartment of Pharmaceutical Chemistry; Macromolecule and Vaccine Stabilization Center; University of Kansas; Lawrence, KS, USACorrespondence[email protected] [email protected]

John M HickeyDepartment of Pharmaceutical Chemistry; Macromolecule and Vaccine Stabilization Center; University of Kansas; Lawrence, KS, USA

Ranajoy MajumdarDepartment of Pharmaceutical Chemistry; Macromolecule and Vaccine Stabilization Center; University of Kansas; Lawrence, KS, USA; Present affiliation: Biopharmaceutical Research and Development; Lilly Research Laboratories; Eli Lilly and Company; Indianapolis, IN, USA

Reza EsfandiaryDepartment of Formulation Sciences; MedImmune LLC; Gaithersburg, MD, USA

Steven M BishopDepartment of Formulation Sciences; MedImmune LLC; Gaithersburg, MD, USA

Hardeep S SamraDepartment of Formulation Sciences; MedImmune LLC; Gaithersburg, MD, USA

C Russell MiddaughDepartment of Pharmaceutical Chemistry; Macromolecule and Vaccine Stabilization Center; University of Kansas; Lawrence, KS, USA

David D WeisDepartment of Chemistry and R.N. Adams Institute of Bioanalytical Chemistry; University of Kansas; Lawrence, KS, USACorrespondence[email protected] [email protected]

David B VolkinDepartment of Pharmaceutical Chemistry; Macromolecule and Vaccine Stabilization Center; University of Kansas; Lawrence, KS, USACorrespondence[email protected] [email protected]

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Hydrogen exchange mass spectrometry reveals protein interfaces and distant dynamic coupling effects during the reversible self-association of an IgG1 monoclonal antibody

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Hydrogen exchange mass spectrometry reveals protein interfaces and distant dynamic coupling effects during the reversible self-association of an IgG1 monoclonal antibody

Supplemental_Material.pdf

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