Kinetics of domain interaction

The Il association state data in the previous section are too preliminary to use in a discussion of the nature of the domain interactions in the or II complementation of 11° or II activities [18,31,32,78]. Therefore, we shall confine ourselves to II.  

Stable heterologous complexes are not necessary to explain the limited P-enolpyr-uvate-dependent mannitol phosphorylation kinetic data now available from domain complementation assays transient complexes between domains are sufficient. The challenge remains, however, to visualize how a subcloned A or B domain would be able to transiently associate with an A or B domain on an dimer or tetramer, 

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