Understanding the thermodynamics that underlie molecular interactions and macromolecular stability is of enormous interest because one can directly relate physical phenomena to tangible numbers. The objective of this study was to probe the conformational change caused by a site specific mutation in a human immunoglobin G (IgG). The two complementary analytical techniques used: Hydrogen-Deuterium Exchange Mass Spectrometry (HDX MS) Differential Scanning Calorimetry (DSC). These analytical tools were used to evaluate the effect of this mutation. Both contributed to the understanding of the structure of this biotherapeutic molecule.

Higher order structure analysis using hydrogen deuterium exchange mass spectrometry (HDX MS) and differential scanning calorimetry (DSC)

251st National Meeting (2016)

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