Subject: Re: CCL:Folding

From: [email-masked] (Arne Elofsson)
Date: Wed, 25 Oct 1995 13:55:17 +0100

In article <[email-masked]> [email-masked] (Dr. David N. Haney) writes:

> 
> Antonio Rosato writes:
> > here is my question: is there a program that allows one to fold a protein
> > of which only the sequence is known, on the basis of the folding of
> > a similar one? How high should be the omology of the two?
> 

I would say if you have 30% sequence identity it is trivial, between
20 % and 30% you should be able to get it mostly correct, while with
less than 20% it is difficult.

> You should have a look at George Rose's recent work:
> 
> 	Srinivasan and Rose, Proteins, 22:81-99 (1995)
> 	Nichols, Rose, Ten Eyck and Zimm, Proteins, 23:38-48 (1995)
> 

Yes, and ofcourse this works very well, and all my crystallogaphic
friends just quit their jobs. :> 

There was an quite interesting discussion about G. Roses methods in
bionet.proteins, I guess if anyone is interested they can look it up
in the bionet archives,  (search for folding, rose, linus).

I guess the conclusion was that, interesting method that works
surprisingly well (on a small test set) for secondary (and some super-
secondary) structure prediction, but does not predict anything about
tertiary structures.

arne

(To think before you speak is as to wipe your ass before you shit.)
-----------------------------------------------------------------
      From: Arne Elofsson           Email: [email-masked]
      WWW:  http://www.doe-mbi.ucla.edu/people/arne/main.html

---

From: [email-masked] (Dr. David N. Haney)
Date: Tue, 24 Oct 1995 10:47:47 -0700 (PDT)

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