IUBio GIL .. BIOSCI/Bionet News .. Biosequences .. Software .. FTP

Empirical knowledge-- structure conservation

Mon Aug 15 09:41:55 EST 1994

Hi to all!

I was thinking... We can't predict the structure of folded proteins (yet)
but it is I guess possible to work our way without this i.e. that we
already have a great collection of proteins tertiary structure and that
various parts of these proteins have specific functionalities that could
be merged so that novel peptides with new properties could be created out
of different peptide chains taken from various proteins.
	For example, let us assume that I wan't to phosphorilate a given
chemical that is an inhibitor of some enzyme. Could I take the binding part
of the second enzyme inhibitor and merge it with a kinase? Would this be
too much of a random process?
	Another question concerns the conservation of tertiary structure:
If I cut a protein in 2 parts, 3 parts, 4 parts... To what extent will the
polypeptide keep its original conformation? Are there any equations
quantifying the lost of original structure in fonction of the length of the 
resultant peptide?

Just wondering...


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