Hydrogen exchange mass spectrometry reveals protein interfaces and distant dynamic coupling effects during the reversible self-association of an IgG1 monoclonal antibody-Reference-Cited by-同舟云学术

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

Published:2015-04-15 Issue:3 Volume:7 Page:525-539
ISSN:1942-0862
Container-title:mAbs
language:en
Short-container-title:mAbs

Author:

Arora Jayant,Hickey John M,Majumdar Ranajoy,Esfandiary Reza,Bishop Steven M,Samra Hardeep S,Middaugh C Russell,Weis David D,Volkin David B

Publisher

Informa UK Limited

Subject

Immunology,Immunology and Allergy

Link

http://www.tandfonline.com/doi/pdf/10.1080/19420862.2015.1029217

Reference82 articles.

1. mAbs

2. Challenges in the development of high protein concentration formulations

3. The Influence of Macromolecular Crowding and Macromolecular Confinement on Biochemical Reactions in Physiological Media

4. Implications of macromolecular crowding for protein assembly

5. Reversible Self-Association Increases the Viscosity of a Concentrated Monoclonal Antibody in Aqueous Solution

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