Protein Folding - How it works? (Jul/03/2008 )

Okay, two articles:

http://www.physorg.com/news134219274.html

and

http://www.physorg.com/news134226755.html

Couple this paragraph from the first:

"That's what the Ohio State chemists find most exciting: the molecule does not maintain only one shape. Depending on its surroundings -- the chemical "nudges" that it receives on the outside -- it will adjust."

with this paragraph from the second:

"Zare's team discovered that as a hydrogen atom passed close to a deuterium molecule, the chemical forces tugged on the nearest of the deuterium atoms in the molecule, pulling it away from the other deuterium atom. But if the tug was not strong enough to break the two deuterium atoms apart, as the hydrogen atom moved farther away its hold on the deuterium atom would weaken. The deuterium atom would eventually slip from its grip and snap back toward the other deuterium atom, initiating an oscillation, or vibration."

So what could be responsible for the multiplicities of protein folding are the "soft" collisions inside the cell between the newly formed peptide chains and ambient elements in the cytoplasm.

Do researchers presently entertain this idea?

Um....Maybe it's because I've worked with a number of people who do molecular moldeling of protein and protein interactions,

but I thought this line of thought was commonly accepted???

When you model a molecule, you have to consider the forces (and distances) surrounding ever atom in the molecule... Some of those forces are from atoms or molecules that pass by, which constantly happens... Water (in the case of protein) being the most prevalent...

No molecule ever stops moving or vibrating... (it would have to be 0 K - absolute freezing at which piont the universe as we know it ceases to be)

Maybe this is actually way over my head and I'm missing the real point... which happens often.. sigh...