Folding Forum

In the August 2010 issue of Scientific American http://www.scientificamerican.com/artic ... ible-in-4d (subscription required for full article), there is quite a bit about the ability to capture femtosecond-scale processes, such as proteins folding. Would this research be helpful in confirming or enhancing the computer models used by FAH?

It will be a revolution in molecular research.

Idk, I would love to be able to read the entire article but I won't pay for a subscription ( and won't ask someone who has to... no I really won't ).

But this comment :

richard busch; no, because electron microscope specimens need to be dead and delicatley prepared. i would love to see it too though!

doesn't sound encouraging.

That is, if that person knows what he is talking about which I have no way of knowing for sure.

Anyone?

MtM wrote:Idk, I would love to be able to read the entire article but I won't pay for a subscription ( and won't ask someone who has to... no I really won't ).

But this comment :

richard busch; no, because electron microscope specimens need to be dead and delicatley prepared. i would love to see it too though!

doesn't sound encouraging.

That is, if that person knows what he is talking about which I have no way of knowing for sure.

Anyone?

The answer quoted above was to the question:

I'd like to see the inner workings of a living animal cell. Is this possible with the 4D electron device?

But I don't believe that a protein is a living cell, and given the reference

We have also imaged individual proteins and cells.

then I would expect there to be a possibilty of this being used to confirm some of the F@H results.
However, a problem might be the conditions in which a protein must be held for study under an electron microscope (temperature, solvent etc.)

I am under the impression, and I can off course be wrong, that f@h can not profit from it because of this:

source

“This demonstration shows that cryo-EM is doable and is a major step in reaching the full potential of this technique,” he said. “The goal is to have it reach a 3 to 4 angstrom resolution, which would allow us to clearly see the amino acids that make up a protein.”

This refers to electron cryomicroscopy, something which would allow studying proteins while being active.

The last line of the quoted article from OP is such:

We have also imaged individual proteins and cells.

To me this reads like it's a still image, and it was confirmed by that comment I linked to. If the scale can only be obtained because the specimen needs to be static ( dead ), it could not confirm anything from the research of PG.

This is way above my pay grade, I admit without hesitation, and I could very well be interpreting the limited information I have wrongly.

This is very neat research. However, it won't replace what we do (it's not high enough spatial resolution), but rather complement it, by giving us more data to test our methods against.