Long ago Geoff Barton talked at a CCP4 study weekend about this in a
molecular replacement session.
You could probably find it on the main CCP4 web page.
Eleanor
Yoder, Marilyn wrote:
My 'googling' skills are failing me and thought perhaps someone here
could point me in the right direction.
I have two questions.
1. It is often stated that with ~30% sequence identity, protein folds
will likely be similar. I can't find a reference to this
'rule-of-thumb'. I suspect there has been a systematic study showing
this to be the case, but I can't put my finger on it.
2. I'm looking for examples where proteins of some size, at least 100
amino acids, have sequence identity of ~30% but do not have similar
folds. Again, I'm having difficulties finding such and would
appreciate any examples anyone can provide. (Wasn't there a contest
or something where investigators were challenged to introduce the
minimal sequence change that generated a 'different' structure?).
Many thanks,
Marilyn Yoder
Marilyn D. Yoder
Division of Cell Biology and Biophysics
University of Missouri-Kansas City
5007 Rockhill Rd.
Kansas City, MO 64110-2499
phone: 816-235-1986
fax: 816-235-1503
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