The studies revealed essential differences in the internal flexibility within and between domains and in the energy of non-covalent interactions between domains and subunits of immunoglobulins of different subclasses and of different animals. The higher extent of non-covalent interactions between the Fab and Fc subunits correlates with the lower extent of interactions between the CH2 and CH3 domains (the higher flexibility of the FC parts). Hapten-binding induces conformational changes in the Fc subunits of the immunoglobulins with strong non-covalent interactions between the Fab and Fc subunits.
|Number of pages||10|
|Publication status||Published - Dec 1 1981|
ASJC Scopus subject areas