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Dear Iris,
we have also seen in the past that designed coiled coils in particular may
form mixtures of oligomers with different multiplicities.
Would you consider fusing your sequence to a small trimerisation
domain (29aa)? If yes, an excellent candidate would be the
'foldon' domain of phage T4 fibritin. The original structure
is Tao et al (1997) Structure 5, 789-798, but you may also
search PDB and Pubmed for 'foldon' and maybe 'fibritin' for the
more recent work including fusions.
Good luck,
Sergei
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Hi there,
I have the following problem: I expressed a designed 67mer peptide/protein
(7.8kd) which we believe forms coiled coils. On SDS-PAGE after crosslinking we
see : monomer, dimer, trimer tetramer and pentamer. I'd like to get the
trimeric form clean and so far I've used size exclusion chromatography superdex
75 column, it doesn't really work, the separation efficiency is practically
non existent in this size range, also I suspect that the rod shape of the
protein doesn't help here. Can anyone suggest a better separation method
between the various multimeric forms? I'd like to get a homogeneous trimeric
form.
Thanks, Iris
--
Prof. Sergei V. Strelkov
Laboratory for Biocrystallography
Department of Pharmaceutical Sciences, O&N 2
Catholic University of Leuven
Herestraat 49 bus 822, B-3000 Leuven, Belgium
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