Subject: protein modeling

From: shawn feaster <[email-masked]>
Date: Fri, 17 Mar 1995 13:07:36 -0600 (CST)

Dear all,

Is it possible to force a complex of 3 proteins to have a triple helix
conformation without having the original tertiary structures?  It is know
from CD that they do form a triple helix complex, the regions of the
proteins which interact are known, and you can also see this from scanning
em.  If this is possible, what software should be used?  I do know that de
novo protein folding is computationally "impossible". 

Thanks,

Shawn Feaster
[email-masked]

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From: Wang Yanli <[email-masked]>
Date: Sat, 18 Mar 1995 10:33:30 +0800 (SST)

Dear netters,

I am interested in protein folding study, indeed I am interested in 
theoritical method. So I need experiment data to test my methods.
I know some examples, such as ribonuclease, BPTI, cytochrome, but
I need more other ones.  

Could anybody provide me examples of proteins, for which  refolding
experiments have been carried out in vitro, I will need not only
successful examples, but as well as those failed. 

Any information from you will be highly appreciated. Thanks a lot in 
advance.

Yanli Wang
Molecular Design Lab.
Peking University
e-mail: [email-masked]