Would a consensus sequence form an active protein? (Cont.)

Neil Clarke Neil.Clarke at qmail.bs.jhu.edu
Wed Mar 2 16:01:23 EST 1994


 >In Article <2kvhqk$cjk at ucunix.san.uc.edu>, naussjl at ucunix.san.uc.edu
> >(Jeffrey L Nauss) wrote:
> >>I am a molecular modeler here at U. Cincinnati lately doing some
> >>structutral homology modeling of proteins.  I was recently looking
> >>over some sequences making comparisons with the consensus sequence
> >>when the question in the subject line struck me.  If one synthesized
> >>an enzyme by whatever means using a consensus sequence, would the
> >>resulting polypeptide fold properly and would it be active?

Jeremy Berg's group has made a consensus zinc finger peptide based on the
125 zinc fingers known at the time (several years ago).  The consensus
sequence behaves in every respect like a "wild type" zinc finger. 
Actually, in some ways (for example Zn dissociation constant) it is better
than any of the wild-type sequences examined.  Keep in mind that this is a
small peptide that requires metal binding to fold stably. IMHO, this better
than wt observation is _not_ going to be generally true.



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