Comment to S.Blocklehurst (Re: Well, ...)

Marianna Max drmax at casbah.acns.nwu.edu
Sun May 7 14:43:22 EST 1995


In article <arneznehzdnajd5r at hodgkin.mbi.ucla.edu>,
Arne Elofsson <arne at hodgkin.mbi.ucla.edu> wrote:
>In article <
>>
>arne
>
>PS. I know what thew question is, so if you know the answer 42, we should be happy.
>    My question is to given any sequence build a model to within 1.0 A from a crustal
>    structure. (At the moment I would be happu with 1.5 or even 2. (-: )
>
>-- 
>--------------------------------------------------------
>               From: Arne Elofsson
>         Email: arne at hodgkin.mbi.ucla.edu   			
>  WWW:  http://www.doe-mbi.ucla.edu/arne/main.html	


Well this is probably a very naive question but chock it up to my not being a
protein chemist. How does one deal with "the protein folding question" and
crystal structure of a protein when in the real world the biologically active
configuration(s) of a protein has some sort of help or history dependence in
reaching that state.

I'll give you an example. I work with a protein that has a number of potential
structures (apparently based on the fact that under different conditions it
behaves differently). This protein is an opsin. In its native state or when it
is expressed in a cell system that apparently has factors that aid its correct
folding (by correct I mean biologically active) it binds 11-cis retinal. When 
it is expressed in apparently inappropriate cells it doesn't fold properly and
doesn't bind 11-cis retinal. Can protein folding models hope to deal with the
requirements for chaperonin-like "helper" proteins in a general model or will
each protein require its own set of rules in order to be solved? 

Max




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