Protein Fossil Formation: A Novel Approach to Studying 3D Structures

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In summary: However, these techniques are not sensitive enough to determine the 3D structure of large proteins. The most sensitive techniques are X-ray crystallography and nuclear magnetic resonance. However, these require the protein to be crystallized first. And, even then, the resolution is not great (typically around 2-3 Angstroms). The technique that has been most successful in solving large proteins in solution is electron microscopy. This technique works because proteins are negatively charged, and the electrons in the electron microscope can be used to image the protein. However, electron microscopy has two major limitations. First, the resolution is low (typically around 10-15 Angstroms). Second, electron microscopy is not
  • #1
mather
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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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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
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
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
mather said:
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.
 

What is "Protein Fossil Formation"?

"Protein Fossil Formation" is a novel approach to studying the 3D structures of proteins. It involves the use of fossilization techniques to preserve proteins, allowing scientists to study their structures and functions in their natural state.

How is this approach different from traditional methods of studying protein structures?

Traditional methods of studying protein structures involve isolating and purifying proteins in a laboratory setting. This can often alter the natural state of the protein and limit the accuracy of the results. Protein fossil formation allows for the study of proteins in their natural environment, providing more accurate and detailed information.

What are the benefits of using protein fossil formation to study protein structures?

There are several benefits to using this approach. Firstly, it allows scientists to study proteins in their natural state, providing a more accurate understanding of their structures and functions. Additionally, it can provide insights into the evolutionary history of proteins and their interactions with other molecules.

What techniques are used in protein fossil formation?

Protein fossil formation involves a combination of techniques, including fossilization using minerals, X-ray crystallography, and electron microscopy. These techniques allow for the preservation and visualization of protein structures in their natural state.

What potential applications does this approach have?

This approach has many potential applications, including the study of ancient proteins in fossils, the analysis of protein structures in environmental samples, and the development of new drugs and therapies based on natural protein structures.

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