Leu Zipper Blues
sbe at biochem.usyd.edu.au
Fri Mar 21 23:37:07 EST 1997
In article <Pine.GSO.3.96.970321100824.18039A-100000 at sun1.oulu.fi>, Pete
<pkursula at cc.oulu.fi> wrote:
|| Suppose that you found out that your protein has a leucine zipper
|| structure and forms tight dimers... Is possible to separate these into
Yes, using denaturing conditions (low pH, urea, GuHCl, etc etc). If your
protein is small enough then you should be able to get pure monomer by
RP-HPLC - see (ahem) Biochemistry 35: 9069-9075 (1996) for how we have done
this for Jun and Fos LZ.
|| On the other hand, if one is studying the function/ligands of
|| the protein in question, is this feasible?
Umm..., feasible in what sense?
||Are these proteins present in the cell ONLY as dimers or is there an
||equilibrium that would enable the monomeric form to also have a distinct
This will depend on the values for the equilibrium constant and the
cellular concentration of your protein - ie, if the concn is much greater
than Kequil, then most will be dimer but most will be monomer if the concn
is much less than Kequil. See Science 245: 646-648 (1989) for a discussion
of this in the case of the Jun and Fos LZ.
Dr Simon B Easterbrook-Smith Voice: (+) 612 9351 3905
Department of Biochemistry FAX: (+) 612 9351 4726
University of Sydney Email: sbe at biochem.usyd.edu.au
Sydney NSW 2006
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easy to understand, wrong, answer.
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