Dear all,
Karen question reminded me that I have one also.
I study a protein that homodimerizes via a long helix. A number of
homologs exist. They all dimerize, but the structure is only known of
the first. Homology is high enough that I can easily thread the
homologs' sequences onto the structure.
How do I go about analyzing the new dimerization interfaces? Before
having Pisa have a go, I'd like to do some sort of minimization to allow
for wiggling of one helix with respect to the other and rotamerization
of side chains. What I'm ultimately interested in is which homologs are
likely to form heterooligomers. There is some experimental evidence for
that.
I'm grateful for suggestions.
Andreas
--
>> Andreas Förster <<
Imperial College London
https://wasatch.biochem.utah.edu/~andreas
