Contribution of the inter-chain disulfide bonds to the conformation and stability of immunoglobulin as revealed by HDX MS

摘要

No significant global conformational change was observed after reduction of inter-chain disulfide bonds. The region immediately after the hinge in the CH2 domain becomes less protected after reduction. More regions in both CH2 and CH3 domains of IgG2 displayed slightly less protection after reduction compared with IgG1. This simple experiment can be used as a model to validate the ability of a HDX MS system to detect minor conformational changes.