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
