Timothy R. Hughes
th035681 at mbcr.bcm.tmc.edu
Wed Oct 19 14:45:32 EST 1994
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?
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