protein aggregation

[Timothy R. Hughes]

Dear Netters,

I am working on the research proposal for my qualifying
exam.  It involves a mouse protein (Mx1) which aggregates
in physiological buffers, and forms dimers and trimers
in dissociating solvents.  I would like to determine if 
aggregation is physiologically important, since the
protein seems to aggregate in the nucleus as well.  From published 
deletion constructs, it appears that C-terminal sequences mediate 
formation of dimers and trimers, but an internal 50 amino acid 
segment close to the N-terminus may mediate aggregation.

Does that make sense?  I have heard of plenty of dimer- 
and multimerization motifs, but I guess I had thought that
aggregation was due to some kind of hydrophobic interaction
having to do with the whole structure, not just a small segment.
Then again, I'm not exactly sure about what exactly makes
other proteins aggregate.  Could 50 residues mediate such a
property?  Are there other aggregation motifs (antibodies?) 
Can anybody point me to a book or article discussing this? 

Thanks,

Tim Hughes