Hi.
The answer to your questions is that it depends on the structure
and the kind of interactions this structure will have with other parts of
the structure, so depends on the case. What you sugest is just possible
but was already done. I can't remember the names but I saw some papers
doing that in nature. If you're interested I'll try to find these articles.
Sincerly yours,
Rafael.
######################################
# Rafael Iosef Najmanovich Szeinfeld #
# Department of Biochemistry #
# University of Sao Paulo, Brasil. #
# E-mail : szeinfel at fox.cce.usp.br #
# szeinfel at snfma1.if.usp.br #
# szeinfel at iris.iq.usp.br #
# 1762545 at cat.cce.usp.br #
######################################
On 15 Aug 1994 guy at HARFANG.LOGIN.QC.CA wrote:
> 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...
>> Guy
>>
