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

@inproceedings{Arora2015HydrogenEM,
  title={Hydrogen exchange mass spectrometry reveals protein interfaces and distant dynamic coupling effects during the reversible self-association of an IgG1 monoclonal antibody},
  author={Jayant Kumar Arora and John M. Hickey and Ranajoy Majumdar and Reza Esfandiary and Steven M. Bishop and Hardeep S Samra and C. Russell Middaugh and David D Weis and David B. Volkin},
  booktitle={mAbs},
  year={2015}
}
There is a need for new analytical approaches to better characterize the nature of the concentration-dependent, reversible self-association (RSA) of monoclonal antibodies (mAbs) directly, and with high resolution, when these proteins are formulated as highly concentrated solutions. In the work reported here, hydrogen exchange mass spectrometry (HX-MS) was used to define the concentration-dependent RSA interface, and to characterize the effects of association on the backbone dynamics of an IgG1… CONTINUE READING
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