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Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain

โœ Scribed by Arnold McAuley; Jaby Jacob; Carl G. Kolvenbach; Kimberly Westland; Hyo Jin Lee; Stephen R. Brych; Douglas Rehder; Gerd R. Kleemann; David N. Brems; Masazumi Matsumura


Book ID
111753087
Publisher
Cold Spring Harbor Laboratory Press
Year
2007
Tongue
English
Weight
472 KB
Volume
17
Category
Article
ISSN
0961-8368

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๐Ÿ“œ SIMILAR VOLUMES


Contribution of variable domains to the
โœ Roxana M. Ionescu; Josef Vlasak; Colleen Price; Marc Kirchmeier ๐Ÿ“‚ Article ๐Ÿ“… 2008 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 354 KB

Temperature-induced unfolding of three humanized IgG1 monoclonal antibodies and their Fab and Fc fragments was monitored by differential scanning calorimetry at neutral pH. With some exceptions, the thermogram of the intact antibody presents two peaks and the transition with the larger experimental