Title: Message
Dear Marilyn,
I forgot to mention that there is a second, follow-up classic by Chothia and Lesk entitled
"The relation between the divergence of sequence and structure in proteins."
EMBO J. 1986 April; 5(4): 823–826.
which actually makes the connection between structural similarity and seq.id. more solid.
 
Savvas
 

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Savvas N. Savvides
Professor of Structural Biology
Laboratory for Protein Biochemistry / Structural Biology Group
Ghent University
K.L.Ledeganckstraat 35, 7th floor
9000 Ghent, BELGIUM
Phone: +32-(0)9-264.51.24 ; +32-(0)472-92.85.19 ; FAX: +32-(0)9-264.53.38
Email: [EMAIL PROTECTED]
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-----Original Message-----
From: [EMAIL PROTECTED] [mailto:[EMAIL PROTECTED] On Behalf Of Yoder, Marilyn
Sent: woensdag 21 september 2005 23:44
To: CCP4 Bulletin Board
Subject: [ccp4bb]: sequence/structure homology

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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