Protein fossil

  • Thread starter mather
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  • #1
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hello!

it is often used and in many cases safely accurate to use enlarged and mechanistic models of proteins in order to study them

given than, trying to elucidate the 3D structure of a protein, I wonder if it would be possible to somehow place the protein inside a material that would surround it, then make that material to somehow "freeze" or solidify, then somehow remove the protein and then study the "solid" material that is left, which ofcourse will have a kind of "fossil" of the protein!

studying that fossil, we could get info about protein's 3D structure!

I know there are many "somehow" in the above thought, but I wonder if that rings a bell to someone and tell me if it has already been attempted, or if it could be implemented with a specific material/method/technology he brought to mind

thanks!

PS: if not for proteins, maybe for any other 3D molecule?
 

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  • #2
chemisttree
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The closest thing I can think of is something called a "molecularly imprinted polymer". I've never heard of anyone studying the cast to correlate 3D structure.
 
  • #3
epenguin
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I guess what you ask corresponds to what's called 'negative staining electron microscopy'.
Yes it is more than attempted, it is quite large-scale literature for proteins.
As you get a 2-D image, a large number of images are generally put together mathematically ('tomography') to get a model of the structure.
Not such fine resolution as X-ray crystallography or NMR yet quite useful.

Here are a couple of articles I quickly googled, but hopefully someone better informed can add to this.

http://www.nature.com/aps/journal/v26/n10/pdf/aps2005169a.pdf

http://www.pnas.org/content/109/4/1098.full.pdf+html
 
  • #4
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interesting thanks

X-ray (maybe NMR too, but me not sure) has the tremendous disadvantage that it cannot show the structure of the protein in a solution, but only after crystallizing

this is what I am thinking of overcoming...
 
  • #5
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interesting thanks

X-ray (maybe NMR too, but me not sure) has the tremendous disadvantage that it cannot show the structure of the protein in a solution, but only after crystallizing

this is what I am thinking of overcoming...
People have been solving protein structures in solution via NMR since the 1980s. Now, there are numerous qualifiers here, but for small globular proteins (under 25 kDa or so), it's fairly routine. Also, small-angle (x-ray) scattering can determine low-resolution "molecular envelopes" of proteins in solution.
 

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