In article <3ggmdi$5j at mace.cc.purdue.edu>, barani at mace.cc.purdue.edu (Barani) writes:
|> IMHO crystallographers are more closer to the truths
|> of a biomolecule than anyone else.
Except, of course, for us NMR people. No packing distotions,
good pictures of flexibility. In fact, differences of
|> a distance of 0.2 A between two non bonded atoms out of
|> 13,000 atoms
are probably meaningless--look at calmodulin for an example of
how precise but wildly inaccurate a crystal structure can be.
|> As of today there is no successful program or algorithm that can
|> model a protein based on sequence and there are a few thousand
|> scientists who would lose their jobs if there is one! And for their
|> sake let there not be one !!
Spoken like a crystallographer. Face it--all structures are done
in support of molecular biology. If the molecular biologists didn't
tell us why it's interesting, we wouldn't bother doing a structure
or know what it means when it's done. If the molecular biologists
could be satisfied with coordinates generated automatically, there
would be no reason for people like us to be doing what we're doing.
The time between now and when those "optimistic molecular modellers"
solve the folding problem is a window of opportunity for us
structural biologists to get ourselves tenured somewhere. :-/
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John Kuszewski || |/ /| ||
johnk at spasm.niddk.nih.gov || / /|| ||
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that's MISTER protein G to you! |/__/| |
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